메뉴 건너뛰기




Volumn 402, Issue 1, 2010, Pages 165-177

Cooperative Binding of MgATP and MgADP in the Trimeric PII Protein GlnK2 from Archaeoglobus fulgidus

Author keywords

GlnK signaling; Isothermal titration calorimetry; Protein crystallography

Indexed keywords

2 OXOGLUTARIC ACID; ADENOSINE DIPHOSPHATE MAGNESIUM; ADENOSINE TRIPHOSPHATE MAGNESIUM; BACTERIAL PROTEIN; PROTEIN GLNK1; PROTEIN GLNK2; PROTEIN GLNK3; UNCLASSIFIED DRUG; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; NITROGEN REGULATORY PROTEIN; PIID REGULATORY PROTEIN, BACTERIA;

EID: 77956176486     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.07.020     Document Type: Article
Times cited : (26)

References (51)
  • 1
    • 0035105144 scopus 로고    scopus 로고
    • II signal transduction proteins, pivotal players in microbial nitrogen control
    • II signal transduction proteins, pivotal players in microbial nitrogen control. Microbiol. Mol. Biol. Rev. 2001, 65:80-108.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 80-108
    • Arcondeguy, T.1    Jack, R.2    Merrick, M.3
  • 2
    • 0017703160 scopus 로고
    • Enzymes of nitrogen-metabolism in legume nodules - purification and properties of NADH-dependent glutamate synthase from lupin nodules
    • Boland M.J., Benny A.G. Enzymes of nitrogen-metabolism in legume nodules - purification and properties of NADH-dependent glutamate synthase from lupin nodules. Eur. J. Biochem. 1977, 79:355-362.
    • (1977) Eur. J. Biochem. , vol.79 , pp. 355-362
    • Boland, M.J.1    Benny, A.G.2
  • 3
    • 0016744341 scopus 로고
    • Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: studies with the continuous-culture technique
    • Senior P.J. Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: studies with the continuous-culture technique. J. Bacteriol. 1975, 123:407-418.
    • (1975) J. Bacteriol. , vol.123 , pp. 407-418
    • Senior, P.J.1
  • 4
    • 0037083882 scopus 로고    scopus 로고
    • Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB
    • Coutts G., Thomas G., Blakey D., Merrick M. Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB. EMBO J. 2002, 21:536-545.
    • (2002) EMBO J. , vol.21 , pp. 536-545
    • Coutts, G.1    Thomas, G.2    Blakey, D.3    Merrick, M.4
  • 5
    • 2642530192 scopus 로고    scopus 로고
    • Global carbon/nitrogen control by PII signal transduction in cyanobacteria: from signals to targets
    • Forchhammer K. Global carbon/nitrogen control by PII signal transduction in cyanobacteria: from signals to targets. FEMS Microbiol. Rev. 2004, 28:319-333.
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 319-333
    • Forchhammer, K.1
  • 7
    • 4344695224 scopus 로고    scopus 로고
    • GlnK effects complex formation between NifA and NifL in Klebsiella pneumoniae
    • Stips J., Thummer R., Neumann M., Schmitz R.A. GlnK effects complex formation between NifA and NifL in Klebsiella pneumoniae. Eur. J. Biochem. 2004, 271:3379-3388.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3379-3388
    • Stips, J.1    Thummer, R.2    Neumann, M.3    Schmitz, R.A.4
  • 8
    • 12444315146 scopus 로고    scopus 로고
    • Interaction of N-acetylglutamate kinase with a PII-Like protein in rice
    • Sugiyama K., Hayakawa T., Kudo T., Ito T., Yamaya T. Interaction of N-acetylglutamate kinase with a PII-Like protein in rice. Plant Cell Physiol. 2004, 45:1768-1778.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1768-1778
    • Sugiyama, K.1    Hayakawa, T.2    Kudo, T.3    Ito, T.4    Yamaya, T.5
  • 10
    • 0032530304 scopus 로고    scopus 로고
    • Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein
    • Jiang P., Peliska J.A., Ninfa A.J. Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein. Biochemistry 1998, 37:12782-12794.
    • (1998) Biochemistry , vol.37 , pp. 12782-12794
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 11
    • 0015835725 scopus 로고
    • Regulation of glutamine synthetase adenylylation and deadenylylation by the enzymatic uridylylation and deuridylylation of the PII regulatory protein
    • Mangum J.H., Magni G., Stadtman E.R. Regulation of glutamine synthetase adenylylation and deadenylylation by the enzymatic uridylylation and deuridylylation of the PII regulatory protein. Arch. Biochem. Biophys. 1973, 158:514-525.
    • (1973) Arch. Biochem. Biophys. , vol.158 , pp. 514-525
    • Mangum, J.H.1    Magni, G.2    Stadtman, E.R.3
  • 12
    • 0036430005 scopus 로고    scopus 로고
    • The GlnD and GlnK homologues of Streptomyces coelicolor A3(2) are functionally dissimilar to their nitrogen regulatory system counterparts from enteric bacteria
    • Hesketh A., Fink D., Gust B., Rexer H.U., Scheel B., Chater K., et al. The GlnD and GlnK homologues of Streptomyces coelicolor A3(2) are functionally dissimilar to their nitrogen regulatory system counterparts from enteric bacteria. Mol. Microbiol. 2002, 46:319-330.
    • (2002) Mol. Microbiol. , vol.46 , pp. 319-330
    • Hesketh, A.1    Fink, D.2    Gust, B.3    Rexer, H.U.4    Scheel, B.5    Chater, K.6
  • 13
    • 4744362881 scopus 로고    scopus 로고
    • Regulation of GlnK activity: modification, membrane sequestration and proteolysis as regulatory principles in the network of nitrogen control in Corynebacterium glutamicum
    • Strosser J., Ludke A., Schaffer S., Kramer R., Burkovski A. Regulation of GlnK activity: modification, membrane sequestration and proteolysis as regulatory principles in the network of nitrogen control in Corynebacterium glutamicum. Mol. Microbiol. 2004, 54:132-147.
    • (2004) Mol. Microbiol. , vol.54 , pp. 132-147
    • Strosser, J.1    Ludke, A.2    Schaffer, S.3    Kramer, R.4    Burkovski, A.5
  • 14
    • 0028011762 scopus 로고
    • The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 is modified by serine phosphorylation and signals the cellular N-status
    • Forchhammer K., Tandeau de Marsac N. The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 is modified by serine phosphorylation and signals the cellular N-status. J. Bacteriol. 1994, 176:84-91.
    • (1994) J. Bacteriol. , vol.176 , pp. 84-91
    • Forchhammer, K.1    Tandeau de Marsac, N.2
  • 15
    • 0032895784 scopus 로고    scopus 로고
    • Characterization of the GlnK protein of Escherichia coli
    • Atkinson M.R., Ninfa A.J. Characterization of the GlnK protein of Escherichia coli. Mol. Microbiol. 1999, 32:301-313.
    • (1999) Mol. Microbiol. , vol.32 , pp. 301-313
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 16
    • 36048991815 scopus 로고    scopus 로고
    • II signal transduction protein controlling nitrogen assimilation. Acts as a sensor of adenylate energy charge in vitro
    • II signal transduction protein controlling nitrogen assimilation. Acts as a sensor of adenylate energy charge in vitro. Biochemistry 2007, 46:12979-12996.
    • (2007) Biochemistry , vol.46 , pp. 12979-12996
    • Jiang, P.1    Ninfa, A.J.2
  • 17
    • 0028061944 scopus 로고
    • Reversible uridylylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator I (NRI or NtrC)
    • Atkinson M.R., Kamberov E.S., Weiss R.L., Ninfa A.J. Reversible uridylylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator I (NRI or NtrC). J. Biol. Chem. 1994, 269:28288-28293.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28288-28293
    • Atkinson, M.R.1    Kamberov, E.S.2    Weiss, R.L.3    Ninfa, A.J.4
  • 18
    • 0000451424 scopus 로고
    • Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli
    • Ninfa A.J., Magasanik B. Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli. Proc. Natl Acad. Sci. USA 1986, 83:5909-5913.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 5909-5913
    • Ninfa, A.J.1    Magasanik, B.2
  • 19
    • 0032530281 scopus 로고    scopus 로고
    • The regulation of Escherichia coli glutamine synthetase revisited: role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state
    • Jiang P., Peliska J.A., Ninfa A.J. The regulation of Escherichia coli glutamine synthetase revisited: role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state. Biochemistry 1998, 37:12802-12810.
    • (1998) Biochemistry , vol.37 , pp. 12802-12810
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 20
    • 34047208419 scopus 로고    scopus 로고
    • Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate
    • Jiang P., Mayo A.E., Ninfa A.J. Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate. Biochemistry 2007, 46:4133-4146.
    • (2007) Biochemistry , vol.46 , pp. 4133-4146
    • Jiang, P.1    Mayo, A.E.2    Ninfa, A.J.3
  • 21
    • 0035688691 scopus 로고    scopus 로고
    • Functional characterization of three GlnB homologs in the photosynthetic bacterium Rhodospirillum rubrum: roles in sensing ammonium and energy status
    • Zhang Y., Pohlmann E.L., Ludden P.W., Roberts G.P. Functional characterization of three GlnB homologs in the photosynthetic bacterium Rhodospirillum rubrum: roles in sensing ammonium and energy status. J. Bacteriol. 2001, 183:6159-6168.
    • (2001) J. Bacteriol. , vol.183 , pp. 6159-6168
    • Zhang, Y.1    Pohlmann, E.L.2    Ludden, P.W.3    Roberts, G.P.4
  • 22
    • 2942628873 scopus 로고    scopus 로고
    • The Synechococcus elongatus P signal transduction protein controls arginine synthesis by complex formation with N-acetyl-l-glutamate kinase
    • Heinrich A., Maheswaran M., Ruppert U., Forchhammer K. The Synechococcus elongatus P signal transduction protein controls arginine synthesis by complex formation with N-acetyl-l-glutamate kinase. Mol. Microbiol. 2004, 52:1303-1314.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1303-1314
    • Heinrich, A.1    Maheswaran, M.2    Ruppert, U.3    Forchhammer, K.4
  • 23
    • 33846106811 scopus 로고    scopus 로고
    • Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 Å
    • Gruswitz F., O'Connell J., Stroud R.M. Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 Å. Proc. Natl Acad. Sci. USA 2007, 104:42-47.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 42-47
    • Gruswitz, F.1    O'Connell, J.2    Stroud, R.M.3
  • 24
    • 34548102139 scopus 로고    scopus 로고
    • The Amt/Mep/Rh family of ammonium transport proteins
    • Andrade S.L., Einsle O. The Amt/Mep/Rh family of ammonium transport proteins. Mol. Membr. Biol. 2007, 24:357-365.
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 357-365
    • Andrade, S.L.1    Einsle, O.2
  • 25
    • 0032508415 scopus 로고    scopus 로고
    • GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition
    • Xu Y., Cheah E., Carr P.D., van Heeswijk W.C., Westerhoff H.V., Vasudevan S.G., Ollis D.L. GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition. J. Mol. Biol. 1998, 282:149-165.
    • (1998) J. Mol. Biol. , vol.282 , pp. 149-165
    • Xu, Y.1    Cheah, E.2    Carr, P.D.3    van Heeswijk, W.C.4    Westerhoff, H.V.5    Vasudevan, S.G.6    Ollis, D.L.7
  • 26
    • 0031779083 scopus 로고    scopus 로고
    • Characterization of the glnK-amtB operon of Azotobacter vinelandii
    • Meletzus D., Rudnick P., Doetsch N., Green A., Kennedy C. Characterization of the glnK-amtB operon of Azotobacter vinelandii. J. Bacteriol. 1998, 180:3260-3264.
    • (1998) J. Bacteriol. , vol.180 , pp. 3260-3264
    • Meletzus, D.1    Rudnick, P.2    Doetsch, N.3    Green, A.4    Kennedy, C.5
  • 27
    • 0033968928 scopus 로고    scopus 로고
    • The glnKamtB operon. A conserved gene pair in prokaryotes
    • Thomas G., Coutts G., Merrick M. The glnKamtB operon. A conserved gene pair in prokaryotes. Trends Genet. 2000, 16:11-14.
    • (2000) Trends Genet. , vol.16 , pp. 11-14
    • Thomas, G.1    Coutts, G.2    Merrick, M.3
  • 28
    • 0028069556 scopus 로고
    • The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane protein and a protein highly similar to the Escherichia coli glnB-encoded PII protein
    • Wray L.V., Atkinson M.R., Fisher S.H. The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane protein and a protein highly similar to the Escherichia coli glnB-encoded PII protein. J. Bacteriol. 1994, 176:108-114.
    • (1994) J. Bacteriol. , vol.176 , pp. 108-114
    • Wray, L.V.1    Atkinson, M.R.2    Fisher, S.H.3
  • 29
    • 33749560851 scopus 로고    scopus 로고
    • In vitro analysis of the Escherichia coli AmtB-GlnK complex reveals a stoichiometric interaction and sensitivity to ATP and 2-oxoglutarate
    • Durand A., Merrick M. In vitro analysis of the Escherichia coli AmtB-GlnK complex reveals a stoichiometric interaction and sensitivity to ATP and 2-oxoglutarate. J. Biol. Chem. 2006, 281:29558-29567.
    • (2006) J. Biol. Chem. , vol.281 , pp. 29558-29567
    • Durand, A.1    Merrick, M.2
  • 30
    • 34948865752 scopus 로고    scopus 로고
    • Specificity and regulation of interaction between the PII and AmtB1 proteins in Rhodospirillum rubrum
    • Wolfe D.M., Zhang Y., Roberts G.P. Specificity and regulation of interaction between the PII and AmtB1 proteins in Rhodospirillum rubrum. J. Bacteriol. 2007, 189:6861-6869.
    • (2007) J. Bacteriol. , vol.189 , pp. 6861-6869
    • Wolfe, D.M.1    Zhang, Y.2    Roberts, G.P.3
  • 31
    • 2542509740 scopus 로고    scopus 로고
    • Studies on the roles of GlnK and GlnB in regulating Klebsiella pneumoniae NifL-dependent nitrogen control
    • Arcondeguy T., van Heeswijk W.C., Merrick M. Studies on the roles of GlnK and GlnB in regulating Klebsiella pneumoniae NifL-dependent nitrogen control. FEMS Microbiol. Lett. 1999, 180:263-270.
    • (1999) FEMS Microbiol. Lett. , vol.180 , pp. 263-270
    • Arcondeguy, T.1    van Heeswijk, W.C.2    Merrick, M.3
  • 33
    • 0031824606 scopus 로고    scopus 로고
    • Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli
    • Atkinson M.R., Ninfa A.J. Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli. Mol. Microbiol. 1998, 29:431-447.
    • (1998) Mol. Microbiol. , vol.29 , pp. 431-447
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 34
    • 27244444582 scopus 로고    scopus 로고
    • Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus
    • Andrade S.L., Dickmanns A., Ficner R., Einsle O. Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus. Proc. Natl Acad. Sci. USA 2005, 102:14994-14999.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 14994-14999
    • Andrade, S.L.1    Dickmanns, A.2    Ficner, R.3    Einsle, O.4
  • 35
    • 33846641311 scopus 로고    scopus 로고
    • The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel
    • Conroy M.J., Durand A., Lupo D., Li X.D., Bullough P.A., Winkler F.K., Merrick M. The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel. Proc. Natl Acad. Sci. USA 2007, 104:1213-1218.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1213-1218
    • Conroy, M.J.1    Durand, A.2    Lupo, D.3    Li, X.D.4    Bullough, P.A.5    Winkler, F.K.6    Merrick, M.7
  • 36
    • 33846505024 scopus 로고    scopus 로고
    • Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake
    • Yildiz O., Kalthoff C., Raunser S., Kühlbrandt W. Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake. EMBO J. 2007, 26:589-599.
    • (2007) EMBO J. , vol.26 , pp. 589-599
    • Yildiz, O.1    Kalthoff, C.2    Raunser, S.3    Kühlbrandt, W.4
  • 37
    • 0035818581 scopus 로고    scopus 로고
    • A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803
    • Irmler A., Forchhammer K. A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803. Proc. Natl Acad. Sci. USA 2001, 98:12978-12983.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12978-12983
    • Irmler, A.1    Forchhammer, K.2
  • 38
    • 0037270294 scopus 로고    scopus 로고
    • Molecular properties of the putative nitrogen sensor PII from Arabidopsis thaliana
    • Smith C.S., Weljie A.M., Moorhead G.B. Molecular properties of the putative nitrogen sensor PII from Arabidopsis thaliana. Plant J. 2003, 33:353-360.
    • (2003) Plant J. , vol.33 , pp. 353-360
    • Smith, C.S.1    Weljie, A.M.2    Moorhead, G.B.3
  • 39
    • 33845942520 scopus 로고    scopus 로고
    • Interaction of the membrane-bound GlnK-AmtB complex with the master regulator of nitrogen metabolism TnrA in Bacillus subtilis
    • Heinrich A., Woyda K., Brauburger K., Meiss G., Detsch C., Stülke J., Forchhammer K. Interaction of the membrane-bound GlnK-AmtB complex with the master regulator of nitrogen metabolism TnrA in Bacillus subtilis. J. Biol. Chem. 2006, 281:34909-34917.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34909-34917
    • Heinrich, A.1    Woyda, K.2    Brauburger, K.3    Meiss, G.4    Detsch, C.5    Stülke, J.6    Forchhammer, K.7
  • 40
    • 0014216968 scopus 로고
    • Intracellular Concentration of Bound and Unbound Magnesium Ions in Escherichia coli
    • Hurwitz C., Rosano C.L. Intracellular Concentration of Bound and Unbound Magnesium Ions in Escherichia coli. J. Biol. Chem. 1967, 242:3719-3722.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3719-3722
    • Hurwitz, C.1    Rosano, C.L.2
  • 41
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 2005, 41:207-334.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-334
    • Studier, F.W.1
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillating mode
    • Otwinowski Z.A.M.W. Processing of X-ray diffraction data collected in oscillating mode. Methods Enzymol. 1996, 276:307-326.
    • (1996) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.A.M.W.1
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 1994, 50:760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 46
    • 74549194551 scopus 로고    scopus 로고
    • Molecular replacement with MOLREP
    • Vagin A., Teplyakov A. Molecular replacement with MOLREP. Acta Crystallogr. D 2010, 66:22-25.
    • (2010) Acta Crystallogr. D , vol.66 , pp. 22-25
    • Vagin, A.1    Teplyakov, A.2
  • 47
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 1997, 53:240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 48
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: the free R value. Methods and applications
    • Brunger A.T. Assessment of phase accuracy by cross validation: the free R value. Methods and applications. Acta Crystallogr. D 1993, 49:24-36.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 24-36
    • Brunger, A.T.1
  • 49
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 51


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.