메뉴 건너뛰기




Volumn 1764, Issue 1, 2006, Pages 122-128

Detection and characterization of merohedral twinning in crystals of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes

Author keywords

Hemihedral twinning; Oxalyl coenzyme A decarboxylase; Thiamin diphosphate; Twin fraction; X ray crystallography

Indexed keywords

BACTERIAL ENZYME; CARBOXYLYASE; COCARBOXYLASE; COENZYME A; MAGNESIUM ION; OXALIC ACID; OXALYL COENZYME A DECARBOXYLASE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 33644838821     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.08.016     Document Type: Article
Times cited : (5)

References (30)
  • 1
    • 84980084953 scopus 로고
    • Pseudo-merohedral twinning. the treatment of overlapped data
    • C.T. Grainger Pseudo-merohedral twinning. The treatment of overlapped data Acta Crystallogr., A 25 1969 427 435
    • (1969) Acta Crystallogr., a , vol.25 , pp. 427-435
    • Grainger, C.T.1
  • 2
    • 0001452420 scopus 로고
    • Simple statistics for intensity data from twinned specimens
    • T.O. Yeates Simple statistics for intensity data from twinned specimens Acta Crystallogr., A 44 Pt. 2 1988 142 144
    • (1988) Acta Crystallogr., a , vol.44 , Issue.PART 2 , pp. 142-144
    • Yeates, T.O.1
  • 3
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • T.O. Yeates Detecting and overcoming crystal twinning Methods Enzymol. 276 1997 344 358
    • (1997) Methods Enzymol. , vol.276 , pp. 344-358
    • Yeates, T.O.1
  • 4
    • 0001319782 scopus 로고
    • Estimation of twinning parameter for twins with exactly superimposed reciprocal lattices
    • D. Britton Estimation of twinning parameter for twins with exactly superimposed reciprocal lattices Acta Crystallogr., A 28 1972 296 297
    • (1972) Acta Crystallogr., a , vol.28 , pp. 296-297
    • Britton, D.1
  • 5
    • 0000042963 scopus 로고
    • Treatment of diffraction data from crystals twinned by merohedry
    • R.G. Fisher, and R.M. Sweet Treatment of diffraction data from crystals twinned by merohedry Acta Crystallogr., A 36 1980 755 760
    • (1980) Acta Crystallogr., a , vol.36 , pp. 755-760
    • Fisher, R.G.1    Sweet, R.M.2
  • 6
    • 0001210234 scopus 로고
    • The probability distribution of X-ray intensities
    • A.J.C. Wilson The probability distribution of X-ray intensities Acta Crystallogr. 2 1949 318 321
    • (1949) Acta Crystallogr. , vol.2 , pp. 318-321
    • Wilson, A.J.C.1
  • 7
    • 0001822424 scopus 로고
    • The identification of twins from intensity statistics
    • E. Stanley The identification of twins from intensity statistics J. Appl. Crystallogr. 5 1972 191 194
    • (1972) J. Appl. Crystallogr. , vol.5 , pp. 191-194
    • Stanley, E.1
  • 8
    • 0242713120 scopus 로고    scopus 로고
    • Twinned crystals and anomalous phasing
    • Z. Dauter Twinned crystals and anomalous phasing Acta Crystallogr., D 59 2003 2004 2016
    • (2003) Acta Crystallogr., D , vol.59 , pp. 2004-2016
    • Dauter, Z.1
  • 9
    • 0001638309 scopus 로고
    • The influence of twinning by merohedry on intensity statistics
    • D.C. Rees The influence of twinning by merohedry on intensity statistics Acta Crystallogr., A 36 1980 578 581
    • (1980) Acta Crystallogr., a , vol.36 , pp. 578-581
    • Rees, D.C.1
  • 10
    • 22844441183 scopus 로고    scopus 로고
    • Escherichia coli MltA: MAD phasing and refinement of a tetartohedrally twinned protein crystal structure
    • T.R. Barends, R.M. de Jong, K.E. van Straaten, A.M. Thunnissen, and B.W. Dijkstra Escherichia coli MltA: MAD phasing and refinement of a tetartohedrally twinned protein crystal structure Acta Crystallogr. D 61 2005 613 621
    • (2005) Acta Crystallogr. D , vol.61 , pp. 613-621
    • Barends, T.R.1    De Jong, R.M.2    Van Straaten, K.E.3    Thunnissen, A.M.4    Dijkstra, B.W.5
  • 11
    • 0345862001 scopus 로고    scopus 로고
    • Oxalobacter formigenes and its role in oxalate metabolism in the human gut
    • C.S. Stewart, S.H. Duncan, and D.R. Cave Oxalobacter formigenes and its role in oxalate metabolism in the human gut FEMS Microbiol. Lett. 230 2004 1 7
    • (2004) FEMS Microbiol. Lett. , vol.230 , pp. 1-7
    • Stewart, C.S.1    Duncan, S.H.2    Cave, D.R.3
  • 13
    • 0037588575 scopus 로고    scopus 로고
    • Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer
    • S. Ricagno, S. Jonsson, N.G. Richards, and Y. Lindqvist Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer EMBO J. 22 2003 3210 3219
    • (2003) EMBO J. , vol.22 , pp. 3210-3219
    • Ricagno, S.1    Jonsson, S.2    Richards, N.G.3    Lindqvist, Y.4
  • 14
    • 0024672742 scopus 로고
    • Purification and characterization of oxalyl-coenzyme a decarboxylase from Oxalobacter formigenes
    • A.L. Baetz, and M.J. Allison Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes J. Bacteriol. 171 1989 2605 2608
    • (1989) J. Bacteriol. , vol.171 , pp. 2605-2608
    • Baetz, A.L.1    Allison, M.J.2
  • 15
    • 0028355157 scopus 로고
    • Molecular cloning, DNA sequence, and gene expression of the oxalyl-coenzyme a decarboxylase gene, oxc, from the bacterium Oxalobacter formigenes
    • H.Y. Lung, A.L. Baetz, and A.B. Peck Molecular cloning, DNA sequence, and gene expression of the oxalyl-coenzyme A decarboxylase gene, oxc, from the bacterium Oxalobacter formigenes J. Bacteriol. 176 1994 2468 2472
    • (1994) J. Bacteriol. , vol.176 , pp. 2468-2472
    • Lung, H.Y.1    Baetz, A.L.2    Peck, A.B.3
  • 16
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • S. Doublié Preparation of selenomethionyl proteins for phase determination Methods Enzymol. 276 1997 523 530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 17
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data Joint CCP4 + ESF-EAMCB Newsl
    • A.G.W. Leslie Recent changes to the MOSFLM package for processing film and image plate data Joint CCP4 + ESF-EAMCB Newsl Protein Crystallogr. 26 1992
    • (1992) Protein Crystallogr. , vol.26
    • Leslie, A.G.W.1
  • 18
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4, the CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4, The CCP4 suite: programs for protein crystallography Acta Crystallogr., D 50 1994 760 763
    • (1994) Acta Crystallogr., D , vol.50 , pp. 760-763
  • 19
    • 0036295208 scopus 로고    scopus 로고
    • Crystal structure of yeast acetohydroxyacid synthase: A target for herbicidal inhibitors
    • S.S. Pang, R.G. Duggleby, and L.W. Guddat Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors J. Mol. Biol. 317 2002 249 262
    • (2002) J. Mol. Biol. , vol.317 , pp. 249-262
    • Pang, S.S.1    Duggleby, R.G.2    Guddat, L.W.3
  • 20
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • A. Vagin, and A. Teplyakov MOLREP: an automated program for molecular replacement J. Appl. Crystallogr. 30 1997 1022 1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 21
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • G.S. French, and K.S. Wilson On the treatment of negative intensity observations Acta Crystallogr., A 34 1978 517 523
    • (1978) Acta Crystallogr., a , vol.34 , pp. 517-523
    • French, G.S.1    Wilson, K.S.2
  • 22
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968
    • (1968) J. Mol. Biol. , vol.33
    • Matthews, B.W.1
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr., A 47 Pt. 2 1991 110 119
    • (1991) Acta Crystallogr., a , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr., D 53 1997 240 255
    • (1997) Acta Crystallogr., D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 26
    • 0000984512 scopus 로고
    • Structure determination of plastocyanin from a specimen with a hemihedral twinning fraction of one-half
    • M.R. Redinbo, and T.O. Yeates Structure determination of plastocyanin from a specimen with a hemihedral twinning fraction of one-half Acta Crystallogr., D 49 1993 375 380
    • (1993) Acta Crystallogr., D , vol.49 , pp. 375-380
    • Redinbo, M.R.1    Yeates, T.O.2
  • 27
    • 0032896789 scopus 로고    scopus 로고
    • On the molecular-replacement problem in the presence of merohedral twinning: Structure of the N-terminal half-molecule of human lactoferrin
    • W.A. Breyer, R.L. Kingston, B.F. Anderson, and E.N. Baker On the molecular-replacement problem in the presence of merohedral twinning: structure of the N-terminal half-molecule of human lactoferrin Acta Crystallogr., D 55 Pt. 1 1999 129 138
    • (1999) Acta Crystallogr., D , vol.55 , Issue.PART 1 , pp. 129-138
    • Breyer, W.A.1    Kingston, R.L.2    Anderson, B.F.3    Baker, E.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.