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1
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0025871254
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Structures of larger proteins: Three-and four-dimensional heteronuclear NMR spectroscopy
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Clore GM, Gronenborn AM: Structures of larger proteins: three-and four-dimensional heteronuclear NMR spectroscopy. Science 1991, 252:1390-1399.
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(1991)
Science
, vol.252
, pp. 1390-1399
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Clore, G.M.1
Gronenborn, A.M.2
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3
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0000225125
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Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy
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Clore GM, Gronenborn AM: Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy. Protein Eng 1987, 1:275-288.
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(1987)
Protein Eng
, vol.1
, pp. 275-288
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Clore, G.M.1
Gronenborn, A.M.2
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4
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0025261972
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Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy
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Dyson HJ, Gippert, GP, Case DA, Holmgren A, Wright PE: Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. Biochemistry 1990, 29:4129-4136.
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(1990)
Biochemistry
, vol.29
, pp. 4129-4136
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Dyson, H.J.1
Gippert, G.P.2
Case, D.A.3
Holmgren, A.4
Wright, P.E.5
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5
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0025909444
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The high resolution three-dimensional structure of reduced recombinant human thioredoxin in solution
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Forman-Kay JD, Clore GM, Wingfield PT, Gronenborn AM: The high resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Biochemistry 1991, 30:2685-2698.
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(1991)
Biochemistry
, vol.30
, pp. 2685-2698
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Forman-Kay, J.D.1
Clore, G.M.2
Wingfield, P.T.3
Gronenborn, A.M.4
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6
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0031019983
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Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coil phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR
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Garrett DS, Seok YJ, Liao DI, Peterkofksy A, Gronenborn AM, Clore GM: Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coil phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Biochemistry 1997, 36:2517-2530. This paper presents the structure determination of one of the first single chain 30 kDa proteins solved by NMR and describes in detail how this was accomplished, including the use of perdeuteration.
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(1997)
Biochemistry
, vol.36
, pp. 2517-2530
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Garrett, D.S.1
Seok, Y.J.2
Liao, D.I.3
Peterkofksy, A.4
Gronenborn, A.M.5
Clore, G.M.6
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7
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0031569799
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The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site
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Martin JR, Mulder FAA, Karimi-Nejad Y, van der Zwan J, Mariani M, Schipper D, Boelens R: The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site. Structure 1997, 5:521-532. This presents the structure determination of one of the first single chain 30 kDa proteins by NMR.
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(1997)
Structure
, vol.5
, pp. 521-532
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Martin, J.R.1
Mulder, F.A.A.2
Karimi-Nejad, Y.3
Van Der Zwan, J.4
Mariani, M.5
Schipper, D.6
Boelens, R.7
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8
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0030902818
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Solution structure of an rRNA methyltransferase (ErmAm) that confers MLS antibiotic resistance
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Yu L, Petros AM, Schnuchel A, Zhong P, Severin JM, Walker K, Holzman TF, Fesik SW: Solution structure of an rRNA methyltransferase (ErmAm) that confers MLS antibiotic resistance. Nat Struct Biol 1997, 4:483-489. This presents the structure determination of one of the first single chain 30 kDa proteins by NMR.
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(1997)
Nat Struct Biol
, vol.4
, pp. 483-489
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-
Yu, L.1
Petros, A.M.2
Schnuchel, A.3
Zhong, P.4
Severin, J.M.5
Walker, K.6
Holzman, T.F.7
Fesik, S.W.8
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9
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0032541424
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Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41
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Caffrey M, Cai M, Kaufman J, Stahl SJ, Wingfield PT, Covell DG, Gronenborn AM, Clore GM: Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41. EMBO J 1998, 17:4572-4584. This paper describes the structure determination of a symmetric 44 kDa trimer. The trimeric nature of the structure makes this a particularly difficult task for NMR, and various NMR experiments for observing intermolecular contacts in proteins of this size are presented.
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(1998)
EMBO J
, vol.17
, pp. 4572-4584
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-
Caffrey, M.1
Cai, M.2
Kaufman, J.3
Stahl, S.J.4
Wingfield, P.T.5
Covell, D.G.6
Gronenborn, A.M.7
Clore, G.M.8
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10
-
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0030826444
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Structure of translation factor EIF4E bound to m7GDP and interaction with 4E-binding protein
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Matsuo H, Li HJ, McGuire AM, Fletcher CM, Gingras AC, Sonenberg N, Wagner G: Structure of translation factor EIF4E bound to m7GDP and interaction with 4E-binding protein. Nat Struct Biol 1997, 4:717-724. This paper describes the use of CHAPS to increase the solubility of a protein and shows that the structure of a protein-micelle complex of ∼40 kDa can be solved by NMR.
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(1997)
Nat Struct Biol
, vol.4
, pp. 717-724
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-
Matsuo, H.1
Li, H.J.2
McGuire, A.M.3
Fletcher, C.M.4
Gingras, A.C.5
Sonenberg, N.6
Wagner, G.7
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12
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0025361336
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Heteronuclear three-dimensional NMR spectroscopy of isotopically labeled biological macromolecules
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Fesik SW, Zuiderweg ERP: Heteronuclear three-dimensional NMR spectroscopy of isotopically labeled biological macromolecules. Q Rev Biophys 1990, 23:97-131.
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(1990)
Q Rev Biophys
, vol.23
, pp. 97-131
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Fesik, S.W.1
Zuiderweg, E.R.P.2
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13
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0002608849
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Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination
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Clore GM, Gronenborn AM: Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination. Prog NMR Spectrosc 1991, 23:43-92.
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(1991)
Prog NMR Spectrosc
, vol.23
, pp. 43-92
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Clore, G.M.1
Gronenborn, A.M.2
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14
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12044252858
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Methodological advances in protein NMR
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Bax A, Grzesiek S: Methodological advances in protein NMR. Accounts Chem Res 1993: 26:131-138.
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(1993)
Accounts Chem Res
, vol.26
, pp. 131-138
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Bax, A.1
Grzesiek, S.2
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15
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0001594959
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Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients
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Bax A, Pochapsky SS: Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients. J Magn Reson 1992, 99:638-643.
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(1992)
J Magn Reson
, vol.99
, pp. 638-643
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Bax, A.1
Pochapsky, S.S.2
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16
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0006925492
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Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
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Kay LE, Keifer P, Saarinen T: Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 1992, 114:10663-10665.
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(1992)
J Am Chem Soc
, vol.114
, pp. 10663-10665
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Kay, L.E.1
Keifer, P.2
Saarinen, T.3
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20
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0031027910
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Global folds of highly deuterated, methyl protonated proteins by multidimensional NMR
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Gardner KH, Rosen MK, Kay LE: Global folds of highly deuterated, methyl protonated proteins by multidimensional NMR. Biochemistry 1997, 36:1389-1401. This paper presents a detailed study of the sort of structures that can be obtained using restraints derived from proteins that are fully perdeuterated with the exception of the amide and methyl groups.
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(1997)
Biochemistry
, vol.36
, pp. 1389-1401
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Gardner, K.H.1
Rosen, M.K.2
Kay, L.E.3
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21
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0030612833
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2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
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2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci USA 1997, 94:12366-12371. This paper describes a simple method, based on the use of constructive intereference between dipole-dipole coupling and chemical shift anisotropy, for eliminating in part one of the major obstacles, namely line broadening due to slow tumbling, for studying large proteins by NMR
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 12366-12371
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Pervushin, K.1
Riek, R.2
Wider, G.3
Wüthrich, K.4
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22
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0030470749
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13C NOE for assignment of NMR lines of larger labeled proteins at larger magnetic fields
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13C NOE for assignment of NMR lines of larger labeled proteins at larger magnetic fields. J Am Chem Soc 1996, 118:12457-12458.
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(1996)
J Am Chem Soc
, vol.118
, pp. 12457-12458
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Fischer, M.W.F.1
Leng, L.2
Zuiderweg, E.R.P.3
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23
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Correlation of connected transitions by two-dimensional NMR spectroscopy
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Griesinger C, Sørensen OW, Ernst RR: Correlation of connected transitions by two-dimensional NMR spectroscopy. J Chem Phys 1986, 85:6837-6852.
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(1986)
J Chem Phys
, vol.85
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Griesinger, C.1
Sørensen, O.W.2
Ernst, R.R.3
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24
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0028673482
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Measurement of homo- and heteronuclear J couplings from quantitative J correlation
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Bax A, Vuister GW, Grzesiek S, Delaglio F, Wang AC. Tschudin R, Zhu G: Measurement of homo- and heteronuclear J couplings from quantitative J correlation. Methods Enzymol 1994, 239:79-105.
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(1994)
Methods Enzymol
, vol.239
, pp. 79-105
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Bax, A.1
Vuister, G.W.2
Grzesiek, S.3
Delaglio, F.4
Wang, A.C.5
Tschudin, R.6
Zhu, G.7
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25
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0029812794
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13C J couplings between carbonyl and carbonyl/carboxyl carbons in isotopically enriched proteins
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13C J couplings between carbonyl and carbonyl/carboxyl carbons in isotopically enriched proteins. J Am Chem Soc 1996, 118:8170-8171.
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(1996)
J Am Chem Soc
, vol.118
, pp. 8170-8171
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Ju, J.S.1
Bax, A.2
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26
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0031111521
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NCγ coupling in isotopically enriched proteins
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NCγ coupling in isotopically enriched proteins. J Biomol NMR 1997, 9:323-328.
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(1997)
J Biomol NMR
, vol.9
, pp. 323-328
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Hu, J.S.1
Bax, A.2
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28
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0032165397
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31P couplings in nucleic acids and protein-nucleic acid complexes by quantitative J correlation spectroscopy
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in press
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31P couplings in nucleic acids and protein-nucleic acid complexes by quantitative J correlation spectroscopy. J Magn Reson 1998, in press.
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(1998)
J Magn Reson
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Clore, G.M.1
Murphy, E.C.2
Gronenborn, A.M.3
Bax, A.4
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29
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33845183709
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1H assignments and their impact on the precision of protein structure determinations in solution
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1H assignments and their impact on the precision of protein structure determinations in solution. J Am Chem Soc 1989, 111:3397-4004.
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(1989)
J Am Chem Soc
, vol.111
, pp. 3397-4004
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Güntert, P.1
Braun, W.2
Billeter, M.3
Wüthrich, K.4
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30
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0025194652
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1H-NMR stereospecific assignments by conformational database searches
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1H-NMR stereospecific assignments by conformational database searches. Biopolymers 1990, 29:813-822.
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(1990)
Biopolymers
, vol.29
, pp. 813-822
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Nilges, M.1
Clore, G.M.2
Gronenborn, A.M.3
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31
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0031000510
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Direct measurement of angles between bond vectors in high-resolution NMR
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Reif B, Hennig M, Griesinger C: Direct measurement of angles between bond vectors in high-resolution NMR. Science 1997, 276:1230-1233. This presents a new method for directly determining angles between bond vectors by measuring the cross-correlated relaxation between two dipolar fields, and applies it to the determination of the backbone torsion angle ψ.
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(1997)
Science
, vol.276
, pp. 1230-1233
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Reif, B.1
Hennig, M.2
Griesinger, C.3
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32
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0031450910
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13C′(carbonyl) chemical shift anisotropy mechanisms
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13C′(carbonyl) chemical shift anisotropy mechanisms. J Am Chem Soc 1997, 119:11938-11940. This paper presents a new method for determining angles between bond vectors by measuring the cross-correlated relaxation between dipolar and chemical shift anisotropy relaxation mechanisms, and applies it to the determination of the backbone torsion angle ψ.
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(1997)
J Am Chem Soc
, vol.119
, pp. 11938-11940
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Yang, D.1
Konrat, R.2
Kay, L.E.3
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33
-
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0025772135
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High resolution three-dimensional structure of interleukin-1 βin solution by three and four dimensional nuclear magnetic resonance spectroscopy
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Clore GM, Wingfield PT, Gronenborn AM: High resolution three-dimensional structure of interleukin-1 βin solution by three and four dimensional nuclear magnetic resonance spectroscopy. Biochemistry 1991, 30:2315-2323.
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(1991)
Biochemistry
, vol.30
, pp. 2315-2323
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Clore, G.M.1
Wingfield, P.T.2
Gronenborn, A.M.3
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34
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0031933143
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Determining the structures of large proteins and protein complexes by NMR
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Clore GM, Gronenborn AM: Determining the structures of large proteins and protein complexes by NMR. Trends Biotechnol 1998, 16:22-34.
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(1998)
Trends Biotechnol
, vol.16
, pp. 22-34
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Clore, G.M.1
Gronenborn, A.M.2
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35
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0030758958
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13Cα chemical shifts and protein backbone conformation
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13Cα shifts and the ψ backbone torsion angle.
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(1997)
J Am Chem Soc
, vol.119
, pp. 8070-8075
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Ottiger, M.1
Bax, A.2
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36
-
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0030000912
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Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases
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Kuszewski J, Gronenborn AM, Clore GM: Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases. Protein Sci 1996, 5:1067-1080.
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(1996)
Protein Sci
, vol.5
, pp. 1067-1080
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Kuszewski, J.1
Gronenborn, A.M.2
Clore, G.M.3
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37
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0031083293
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Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids
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Kuszewski J, Gronenborn AM, Clore GM: Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. J Magn Reson 1997, 125:171-177.
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(1997)
J Magn Reson
, vol.125
, pp. 171-177
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Kuszewski, J.1
Gronenborn, A.M.2
Clore, G.M.3
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38
-
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0030963093
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Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy
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2 ratios can be used as restraints that define long-range order a priori, and applies it to the two domain, 30 kDa protein enzyme I.
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(1997)
Nat Struct Biol
, vol.4
, pp. 443-449
-
-
Tjandra, N.1
Garrett, D.S.2
Gronenborn, A.M.3
Bax, A.4
Clore, G.M.5
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39
-
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0030612335
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13C couplings in structure determination of magnetically oriented macromolecules in solution
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13C couplings in structure determination of magnetically oriented macromolecules in solution. Nat Struct Biol 1997, 4:732-738. This paper describes how dipolar couplings arising from magnetic susceptibility anisotropy can be used to provide restraints that define long-range order a priori, and applies it to a complex of the transcription factor GATA-1 with DNA. It is shown that incorporation of N-H and Cα-H dipolar couplings results in a significant increase in the percentage of residues in the most favourable region of the Ramachandran φ,ψ map.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 732-738
-
-
Tjandra, N.1
Omichinski, J.G.2
Gronenborn, A.M.3
Clore, G.M.4
Bax, A.5
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40
-
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0032012610
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Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude
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Clore GM, Gronenborn AM, Tjandra N: Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude. J Magn Reson 1998, 131:159-162. This paper provides details of how to refine structures against dipolar couplings.
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(1998)
J Magn Reson
, vol.131
, pp. 159-162
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Clore, G.M.1
Gronenborn, A.M.2
Tjandra, N.3
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41
-
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0030722243
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Direct measurement of distances and angles in biomolecules by NMR in dilute liquid crystalline medium
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Tjandra N, Bax A: Direct measurement of distances and angles in biomolecules by NMR in dilute liquid crystalline medium. Science 1997, 278:1111-1114. This paper describes how moderate degrees of alignment while retaining the resolution, sensitivity and simplicity of the isotropic NMR spectrum, can be obtained by the use of a dilute liquid crystalline medium of bicelles, thereby permitting the measurement of a wide range of dipolar couplings.
-
(1997)
Science
, vol.278
, pp. 1111-1114
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Tjandra, N.1
Bax, A.2
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42
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0032174883
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Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings of macromolecules
-
in press
-
Ottiger M, Bax A: Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings of macromolecules. J Biomol NMR 1998, in press. This paper describes in detail how to prepare bicelles for orienting macromolecules and characterizes the ranges of concentration, temperature, pH and salt over which the liquid crystalline phase is stable.
-
(1998)
J Biomol NMR
-
-
Ottiger, M.1
Bax, A.2
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43
-
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0026774489
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Characterization of magnetically orientable bilayers in mixtures of dihexanoylphophatidylcholine and dimyristoylphophatidylcholine by solid-state NMR
-
Sanders CR, Schwonek JP: Characterization of magnetically orientable bilayers in mixtures of dihexanoylphophatidylcholine and dimyristoylphophatidylcholine by solid-state NMR. Biochemistry 1992, 31:8898-8905.
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(1992)
Biochemistry
, vol.31
, pp. 8898-8905
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Sanders, C.R.1
Schwonek, J.P.2
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44
-
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0032478523
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The solution structure of a fungal AREA protein-DNA complex reveals an alternative binding mode for the basic carboxyl tail of GATA factors
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Starich MR, Wikström M, Arst HN, Clore GM, Gronenborn AM: The solution structure of a fungal AREA protein-DNA complex reveals an alternative binding mode for the basic carboxyl tail of GATA factors. J Mol Biol 1998, 277:605-620. Refinement against dipolar couplings is shown to play a key role in the ability to determine the conformation of the carboxyl-terminal tail, which binds in the minor groove of the DNA.
-
(1998)
J Mol Biol
, vol.277
, pp. 605-620
-
-
Starich, M.R.1
Wikström, M.2
Arst, H.N.3
Clore, G.M.4
Gronenborn, A.M.5
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45
-
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0032478541
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The solution structure of the leu22→val mutant AREA DNA binding domain complexed with a TGATAG core element defines a role for hydrophobic packing in the determination of specificity
-
Starich MR, Wikström M, Schumacher S, Arst HN, Gronenborn AM, Clore GM: The solution structure of the leu22→val mutant AREA DNA binding domain complexed with a TGATAG core element defines a role for hydrophobic packing in the determination of specificity. J Mol Biol 1998, 277:621-634.
-
(1998)
J Mol Biol
, vol.277
, pp. 621-634
-
-
Starich, M.R.1
Wikström, M.2
Schumacher, S.3
Arst, H.N.4
Gronenborn, A.M.5
Clore, G.M.6
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46
-
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0031848334
-
Solution structure of cyanovirin-N, a potent HIV-inactivating protein from the cyanobacterium Nostoc ellipsosporum
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N-C′ dipolar coupling. It is shown that this increases the precision of the resulting structures.
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(1998)
Nat Struct Biol
, vol.5
, pp. 571-578
-
-
Bewley, C.A.1
Gustafson, K.R.2
Boyd, M.R.3
Covell, D.G.4
Bax, A.5
Clore, G.M.6
Gronenborn, A.M.7
-
47
-
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0000041884
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Determining the magnitude of the fully asymmetric diffusion tensor from heteronuclear relaxation data in the absence of structural information
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2 ratios for refinement, but also enables one to derive information on the hydrodynamic properties and shape of the macromolecule under consideration.
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(1998)
J Am Chem Soc
, vol.120
, pp. 4889-4890
-
-
Clore, G.M.1
Gronenborn, A.M.2
Szabo, A.3
Tjandra, N.4
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48
-
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0032113480
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A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information
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Clore GM, Gronenborn AM, Bax A: A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J Magn Reson 1998, 133:216-221. It is shown that the magnitude of the fully asymmetric alignment tensor can be obtained in the absence of any structural information by examining the distribution of measured dipolar couplings, which has a powder pattern appearance. It is demonstrated that the accuracy with which the magnitude of the tensor can be obtained is improved by making use of several different dipolar couplings and normalizing them, thereby ensuring a more uniform distribution of vectors.
-
(1998)
J Magn Reson
, vol.133
, pp. 216-221
-
-
Clore, G.M.1
Gronenborn, A.M.2
Bax, A.3
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49
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0030778008
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Probing molecular motion by NMR
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Palmer AG: Probing molecular motion by NMR. Curr Opin Struct Biol 1997, 7:732-737. This is a thorough review of recent advances in the study of dynamics by NMR.
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(1997)
Curr Opin Struct Biol
, vol.7
, pp. 732-737
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-
Palmer, A.G.1
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50
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0032517327
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Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses
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in press
-
Clove GM, Starich MA, Gronenborn AM: Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses. J Am Chem Soc 1998, in press. This paper describes how moderate degrees of alignment, permitting the successful measurement of residual dipolar couplings, can readily be obtained using colloidal suspensions of filamentous phage such as fd or tobacco mosaic virus. It is also shown that virus particles can be used successfully in cases where bicelles are unstable (either becuase of interaction with the protein or because of solution conditions such as pH and temperature), and that the nematic phase is maintained over a wide range of pH and temperature.
-
(1998)
J Am Chem Soc
-
-
Clove, G.M.1
Starich, M.A.2
Gronenborn, A.M.3
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51
-
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0031720496
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Solution structure of the cellular factor of BAF responsible for protecting retroviral DNA from autointegration
-
in press
-
Cai M, Yuang Y, Zheng R, Wei SQ, Ghirlando R, Lee MS, Craigie R, Gronenborn AM, Clore GM: Solution structure of the cellular factor of BAF responsible for protecting retroviral DNA from autointegration. Nat Struct Biol 1998, in press. This paper describes the first example of the use of multiple dipolar coupling refinement for the structure determination of a dimeric protein. In such cases, the dipolar couplings can uniquely define the relative orientation of the subunits.
-
(1998)
Nat Struct Biol
-
-
Cai, M.1
Yuang, Y.2
Zheng, R.3
Wei, S.Q.4
Ghirlando, R.5
Lee, M.S.6
Craigie, R.7
Gronenborn, A.M.8
Clore, G.M.9
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