Reproducible improvements in order and diffraction limit of crystals of bovine mitochondrial F1-ATPase by controlled dehydration

被引：29

作者：

Bowler, Matthew W.

Montgomery, Martin G.

Leslie, Andrew G. W.

Walker, John E. ^{[1
]}

机构：

[1] MRC, Dunn Human Nutr Unit, Cambridge, England

[2] MRC, Mol Biol Lab, Cambridge, England

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2006年 / 62卷

基金：

英国医学研究理事会;

关键词：

D O I：

10.1107/S0907444906020877

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Orthorhombic crystals of bovine F-1-ATPase have been subjected to controlled dehydration. A decrease in the relative humidity surrounding the crystals to 90% reproducibly reduced their unit-cell volume by 22% (950 000 angstrom(3)) and improved the diffraction limit and mosaic spread of the crystals significantly. These dehydrated crystals diffracted X--rays to 1.8 angstrom resolution at a synchrotron source, the best diffraction limit yet attained with these crystals, although radiation damage limited the resolution of a complete data set to 1.95 angstrom.

引用

收藏

页码：991 / 995

页数：5

相关论文

共 24 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] How azide inhibits ATP hydrolysis by the F-ATPases [J].

Bowler, Matthew W. ;

Montgomery, Martin G. ;

Leslie, Andrew G. W. ;

Walker, John E. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (23) :8646-8649

[3] Structure of bovine mitochondrial F1-ATPase inhibited by Mg2+ADP and aluminium fluoride [J].

Braig, K ;

Menz, RI ;

Montgomery, MG ;

Leslie, AGW ;

Walker, JE .

STRUCTURE, 2000, 8 (06) :567-573

[4] 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

[5] Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine [J].

Dobbek, H ;

Gremer, L ;

Meyer, O ;

Huber, R .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (16) :8884-8889

[6] The crystal structure of dipeptidyl peptidase IV(CD26) reveals its functional regulation and enzymatic mechanism [J].

Engel, M ;

Hoffmann, T ;

Wagner, L ;

Wermann, M ;

Heiser, U ;

Kiefersauer, R ;

Huber, R ;

Bode, W ;

Demuth, HU ;

Brandstetter, H .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (09) :5063-5068

[7] 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

[8] Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue [J].

Estébanez-Perpiñá, E ;

Fuentes-Prior, P ;

Belorgey, D ;

Braun, M ;

Kiefersauer, R ;

Maskos, K ;

Huber, R ;

Rubin, H ;

Bode, W .

BIOLOGICAL CHEMISTRY, 2000, 381 (12) :1203-1214

[9]

Gibbons C, 2000, NAT STRUCT BIOL, V7, P1055

[10] The crystal structure of the proprotein processing proteinase furin explains its stringent specificity [J].

Henrich, S ;

Cameron, A ;

Bourenkov, GP ;

Kiefersauer, R ;

Huber, R ;

Lindberg, I ;

Bode, W ;

Than, ME .

NATURE STRUCTURAL BIOLOGY, 2003, 10 (07) :520-526