Escherichia coli MltA:: MAD phasing and refinement of a tetartohedrally twinned protein crystal structure

被引：18

作者：

Barends, TRM ^{[1
]}

de Jong, RM ^{[1
]}

van Straaten, KE ^{[1
]}

Thunnissen, AMWH ^{[1
]}

Dijkstra, BW ^{[1
]}

机构：

[1] Univ Groningen, Biophys Chem Lab, NL-9747 AG Groningen, Netherlands

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2005年 / 61卷

关键词：

D O I：

10.1107/S0907444905005743

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Crystals were grown of a mutant form of the bacterial cell-wall maintenance protein MltA that diffracted to 2.15 angstrom resolution. When phasing with molecular replacement using the native structure failed, selenium MAD was used to obtain initial phases. However, after MAD phasing the crystals were found to be tetartohedrally twinned, hampering correct space-group determination and refinement. A refinement protocol was designed to take tetartohedral twinning into account and was successfully applied to refine the structure. The refinement protocol is described and the reasons for the failure of molecular replacement and the success of MAD are discussed in terms of the effects of the tetartohedral twinning.

引用

页码：613 / 621

页数：9

共 28 条

[1]

[Anonymous], ACTA CRYSTALLOGR D

[2] Acetobacter turbidans α-amino acid ester hydrolase:: merohedral twinning in P21 obscured by pseudo-translational NCS [J].

Barends, TRM ;

Dijkstra, BW .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2003, 59 :2237-2241

[3]

Brunger AT, 1998, ACTA CRYSTALLOGR D, V54, P905, DOI 10.1107/s0907444998003254

[4] Analysis and characterization of data from twinned crystals [J].

Chandra, N ;

Acharya, KR ;

Moody, PCE .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1999, 55 :1750-1758

[5] A novel approach to crystallising proteins under oil [J].

DArcy, A ;

Elmore, C ;

Stihle, M ;

Johnston, JE .

JOURNAL OF CRYSTAL GROWTH, 1996, 168 (1-4) :175-180

[6] Twinned crystals and anomalous phasing [J].

Dauter, Z .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2003, 59 :2004-2016

[7] Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site [J].

de Jong, RM ;

Tiesinga, JJW ;

Rozeboom, HJ ;

Kalk, KH ;

Tang, L ;

Janssen, DB ;

Dijkstra, BW .

EMBO JOURNAL, 2003, 22 (19) :4933-4944

[8] A twinned monoclinic crystal form of human peroxiredoxin 5 with eight molecules in the asymmetric unit [J].

Declercq, JP ;

Evrard, C .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2001, 57 :1829-1835

[9] STRUCTURE OF DEOXYHEMOGLOBIN OF THE ANTARCTIC FISH PAGOTHENIA-BERNACCHII WITH AN ANALYSIS OF THE STRUCTURAL BASIS OF THE ROOT EFFECT BY COMPARISON OF THE LIGANDED AND UNLIGANDED HEMOGLOBIN STRUCTURES [J].

ITO, N ;

KOMIYAMA, NH ;

FERMI, G .

JOURNAL OF MOLECULAR BIOLOGY, 1995, 250 (05) :648-658

[10] Processing of X-ray diffraction data collected in oscillation mode [J].

Otwinowski, Z ;

Minor, W .

MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 :307-326

← 1 2 3 →