Reproducible improvements in order and diffraction limit of crystals of bovine mitochondrial F(1)-ATPase by controlled dehydration.
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.
Bowler
Matthew W
MW
The Medical Research Council Dunn Human Nutrition Unit, Cambridge, England.
Montgomery
Martin G
MG
Leslie
Andrew G W
AG
Walker
John E
JE
D000251:Adenosine Triphosphatases; D000818:Animals; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D003681:Dehydration; D008928:Mitochondria / Q000201:enzymology*; D008958:Models, Molecular; D015233:Models, Statistical; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D015203:Reproducibility of Results; D013367:Submitochondrial Particles / Q000737:chemistry; D013997:Time Factors
D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases