Increasing the diffraction limit and internal order of a membrane protein crystal by dehydration

被引：23

作者：

Kuo, A ^{[1
]}

Bowler, MW ^{[1
]}

Zimmer, J ^{[1
]}

Antcliff, JF ^{[1
]}

Doyle, DA ^{[1
]}

机构：

[1] Univ Oxford, Dept Biochem, Mol Biophys Lab, Oxford OX1 3QU, England

来源：

JOURNAL OF STRUCTURAL BIOLOGY | 2003年 / 141卷 / 02期

基金：

英国惠康基金;

关键词：

chloride channel; crystal; dehydration; membrane protein;

D O I：

10.1016/S1047-8477(02)00633-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

It is notoriously difficult to produce crystals of membrane proteins that diffract to sufficient resolution for structural studies by Xray crystallography. Crystals of a prokaryotic CLC chloride channel that were initially unacceptable for structural analysis improved in both quality and diffraction limit by a process of dehydration. The loss of water decreased the dimensions of the unit cell axes by up to 25 Angstrom, improved the diffraction limit from 8.0 to 4.0 Angstrom, and decreased the mosaicity to values of approximately 1degrees. Dehydration of integral membrane protein crystals should be one of the procedures included in the initial screening for appropriate crystals and as a method of improving the diffraction limits of existing crystals. (C) 2003 Elsevier Science (USA). All rights reserved.

引用

页码：97 / 102

页数：6

共 33 条

[1] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].

ABRAHAMS, JP ;

LESLIE, AGW ;

LUTTER, R ;

WALKER, JE .

NATURE, 1994, 370 (6491) :621-628

[2] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].

BAILEY, S .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763

[3] Structure of the MscL homolog from Mycobacterium tuberculosis:: A gated mechanosensitive ion channel [J].

Chang, G ;

Spencer, RH ;

Lee, AT ;

Barclay, MT ;

Rees, DC .

SCIENCE, 1998, 282 (5397) :2220-2226

[4] Crystallization in cubo:: general applicability to membrane proteins [J].

Chiu, ML ;

Nollert, P ;

Loewen, MC ;

Belrhali, H ;

Pebay-Peyroula, E ;

Rosenbusch, JP ;

Landau, EM .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2000, 56 :781-784

[5] Architecture of RNA polymerase II and implications for the transcription mechanism [J].

Cramer, P ;

Bushnell, DA ;

Fu, JH ;

Gnatt, AL ;

Maier-Davis, B ;

Thompson, NE ;

Burgess, RR ;

Edwards, AM ;

David, PR ;

Kornberg, RD .

SCIENCE, 2000, 288 (5466) :640-649

[6] Structural basis of transcription:: RNA polymerase II at 2.8 Ångstrom resolution [J].

Cramer, P ;

Bushnell, DA ;

Kornberg, RD .

SCIENCE, 2001, 292 (5523) :1863-1876

[7] X-RAY STRUCTURE-ANALYSIS OF A MEMBRANE-PROTEIN COMPLEX - ELECTRON-DENSITY MAP AT 3A RESOLUTION AND A MODEL OF THE CHROMOPHORES OF THE PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS-VIRIDIS [J].

DEISENHOFER, J ;

EPP, O ;

MIKI, K ;

HUBER, R ;

MICHEL, H .

JOURNAL OF MOLECULAR BIOLOGY, 1984, 180 (02) :385-398

[8] The structure of the potassium channel:: Molecular basis of K+ conduction and selectivity [J].

Doyle, DA ;

Cabral, JM ;

Pfuetzner, RA ;

Kuo, AL ;

Gulbis, JM ;

Cohen, SL ;

Chait, BT ;

MacKinnon, R .

SCIENCE, 1998, 280 (5360) :69-77

[9] X-ray structure of a CIC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity [J].

Dutzler, R ;

Campbell, EB ;

Cadene, M ;

Chait, BT ;

MacKinnon, R .

NATURE, 2002, 415 (6869) :287-294

[10] Continuous and discontinuous changes in the unit cell of HIV-1 reverse transcriptase crystals on dehydration [J].

Esnouf, RM ;

Ren, JS ;

Garman, EF ;

Somers, DO ;

Ross, CK ;

Jones, EY ;

Stammers, DK ;

Stuart, DI .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1998, 54 :938-953

← 1 2 3 4 →