메뉴 건너뛰기




Volumn 7, Issue 7, 1999, Pages

Selenium-based MAD phasing: Setting the sites on larger structures

Author keywords

[No Author keywords available]

Indexed keywords

SELENIUM;

EID: 0033565931     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80096-3     Document Type: Review
Times cited : (42)

References (31)
  • 1
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W.A. (1991 ). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 2
    • 0031903288 scopus 로고    scopus 로고
    • MAD phasing grows up
    • Ogata, C.M. (1998). MAD phasing grows up. Nat. Struct. Biol. 5, 638-640.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 638-640
    • Ogata, C.M.1
  • 3
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multi-wavelength anomalous diffraction (MAD) - A vehicle for direct determination of 3-dimensional structure
    • Hendrickson, W.A., Horton, J.R. & LeMaster, D.M. (1990). Selenomethionyl proteins produced for analysis by multi-wavelength anomalous diffraction (MAD) - A vehicle for direct determination of 3-dimensional structure. EMBO J. 9, 1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 4
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublié, S. (1997). Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-530.
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 5
    • 0029643796 scopus 로고
    • Charge coupled device X-ray detectors for macromolecular crystallography
    • Gruner, S.M. & Ealick, S.E. (1995). Charge coupled device X-ray detectors for macromolecular crystallography. Structure 3, 13-15.
    • (1995) Structure , vol.3 , pp. 13-15
    • Gruner, S.M.1    Ealick, S.E.2
  • 6
    • 0028774714 scopus 로고
    • Cryocrystallography
    • Rodgers, D.W. (1994). Cryocrystallography. Structure 2, 1135-1140.
    • (1994) Structure , vol.2 , pp. 1135-1140
    • Rodgers, D.W.1
  • 8
    • 0031045587 scopus 로고    scopus 로고
    • Patterson superposition and ab initio phasing
    • Sheldrick, G.M. (1997). Patterson superposition and ab initio phasing. Methods Enzymol. 276, 628-641.
    • (1997) Methods Enzymol. , vol.276 , pp. 628-641
    • Sheldrick, G.M.1
  • 9
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MAD and MIR
    • Terwilliger, T.C. & Berendzen, J. (1999). Automated structure solution for MAD and MIR. Acta Crystallogr. D 55, 849-861.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 10
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T., et al., & Warren, G.L. (1998). Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 11
    • 80055004570 scopus 로고
    • Generalized method of determining heavy-atom positions using the difference Patterson function
    • Terwilliger, T.C., Kim, S.-H. & Eisenberg, D. (1987). Generalized method of determining heavy-atom positions using the difference Patterson function. Acta Crystallogr. A 43, 1-5.
    • (1987) Acta Crystallogr. A , vol.43 , pp. 1-5
    • Terwilliger, T.C.1    Kim, S.-H.2    Eisenberg, D.3
  • 12
    • 84943920736 scopus 로고
    • Phase annealing in SHELX-90 - Direct methods for larger structures
    • Sheldrick, G.M. (1990). Phase annealing in SHELX-90 - Direct methods for larger structures. Acta Crystallogr. A 46, 467-473.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 467-473
    • Sheldrick, G.M.1
  • 13
    • 84944816270 scopus 로고
    • On the application of phase relationships to complex structures. XVIII. RANTAN - Random MULTAN
    • Yao, J-X. (1983). On the application of phase relationships to complex structures. XVIII. RANTAN - Random MULTAN. Acta Crystallogr. A 37, 35-37.
    • (1983) Acta Crystallogr. A , vol.37 , pp. 35-37
    • Yao, J.-X.1
  • 14
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB version 2.0
    • Weeks, C.M. & Miller, R. (1999). The design and implementation of SnB version 2.0. J. Appl. Crystallogr. 32, 120-124.
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 15
    • 0002272684 scopus 로고    scopus 로고
    • SHELX: Applications to macromolecules
    • (Fortier, S., ed.), Kluwer Academic Publishers, Dordecht, Germany
    • Sheldrick, G.M. (1998). SHELX: Applications to macromolecules. Direct Methods for Solving Structures. (Fortier, S., ed.), pp. 401-411, Kluwer Academic Publishers, Dordecht, Germany.
    • (1998) Direct Methods for Solving Structures , pp. 401-411
    • Sheldrick, G.M.1
  • 17
    • 0032482993 scopus 로고    scopus 로고
    • The shake-and-bake structure determination of triclinic lysozyme
    • Deacon, A.M., Weeks, C.M., Miller, R. & Ealick, S.E. (1998). The shake-and-bake structure determination of triclinic lysozyme. Proc. Natl Acad. Sec. 95, 9284-9289.
    • (1998) Proc. Natl Acad. Sec. , vol.95 , pp. 9284-9289
    • Deacon, A.M.1    Weeks, C.M.2    Miller, R.3    Ealick, S.E.4
  • 19
    • 0001763933 scopus 로고    scopus 로고
    • Difference structure factor normalization for heavy atom or anomalous scattering substructure determinations
    • in press
    • Blessing, R.H. & Smith, G.D. (1999). Difference structure factor normalization for heavy atom or anomalous scattering substructure determinations. J. Appl. Crystallogr., in press.
    • (1999) J. Appl. Crystallogr.
    • Blessing, R.H.1    Smith, G.D.2
  • 21
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • De La Fortelle, E. & Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 22
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), SERC, Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1991 ). Maximum likelihood refinement of heavy atom parameters. In Isomorphous Replacement and Anomalous Scattering. (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), pp. 80-86, SERC, Daresbury Laboratory, Warrington, UK.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 23
    • 0031045818 scopus 로고    scopus 로고
    • Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement
    • Ramakrishnan, V. & Biou, V. (1997). Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement. Methods Enzymol. 276, 538-557.
    • (1997) Methods Enzymol. , vol.276 , pp. 538-557
    • Ramakrishnan, V.1    Biou, V.2
  • 24
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R. & Lamzin, V.S. (1999). Automated protein model building combined with iterative structure refinement, Nat. Struct. Biol. 6, 458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 25
    • 0032813519 scopus 로고    scopus 로고
    • First picture of all the major components of 2-oxo acid dehydrogenase multienzyme complexes obtained by the crystal structure of 2-oxoisovalerate dehydrogenase
    • in press
    • Ævarsson, A., Seger, K., Turley, S., Sokatch, J.R. & Hol, W.G.J. (1999). First picture of all the major components of 2-oxo acid dehydrogenase multienzyme complexes obtained by the crystal structure of 2-oxoisovalerate dehydrogenase. Nat. Struct. Biol., in press.
    • (1999) Nat. Struct. Biol.
    • Ævarsson, A.1    Seger, K.2    Turley, S.3    Sokatch, J.R.4    Hol, W.G.J.5
  • 26
    • 0033134691 scopus 로고    scopus 로고
    • The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 Å resolution reveals a novel fold
    • Ekstrom, J.L., Mathews, I.I., Stanley, B.A., Pegg, A.E. & Ealick, S.E. (1999). The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 Å resolution reveals a novel fold. Structure 7, 583-595.
    • (1999) Structure , vol.7 , pp. 583-595
    • Ekstrom, J.L.1    Mathews, I.I.2    Stanley, B.A.3    Pegg, A.E.4    Ealick, S.E.5
  • 29
    • 0001007592 scopus 로고    scopus 로고
    • X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM) from the E. Coli purine biosynthetic pathway at 2.5 Å resolution
    • in press
    • Li, C., Kappock, T.J., Stubbe, J. & Ealick, S.E. (1999). X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM) from the E. Coli purine biosynthetic pathway at 2.5 Å resolution. Structure, in press.
    • (1999) Structure
    • Li, C.1    Kappock, T.J.2    Stubbe, J.3    Ealick, S.E.4
  • 30
    • 0031947190 scopus 로고    scopus 로고
    • Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength
    • Turner, M.A., Yuan C.S., Borchardt, R.T., Hershfield, M.S., Smith, G.D. & Howell, P.L. (1998). Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat. Struct. Biol. 5, 369-376.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 369-376
    • Turner, M.A.1    Yuan, C.S.2    Borchardt, R.T.3    Hershfield, M.S.4    Smith, G.D.5    Howell, P.L.6
  • 31
    • 0033524982 scopus 로고    scopus 로고
    • Oligomeric structure of the human EphB2 receptor SAM domain
    • Thanos, C.D., Goodwill, K.E. & Bowie, J.U. (1999). Oligomeric structure of the human EphB2 receptor SAM domain. Science 282, 833-836.
    • (1999) Science , vol.282 , pp. 833-836
    • Thanos, C.D.1    Goodwill, K.E.2    Bowie, J.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.