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In situ data collection and structure refinement from microcapillary protein crystallization.

ABSTRACT: In situ X-ray data collection has the potential to eliminate the challenging task of mounting and cryocooling often fragile protein crystals, reducing a major bottleneck in the structure determination process. An apparatus used to grow protein crystals in capillaries and to compare the background X-ray scattering of the components, including thin-walled glass capillaries against Teflon, and various fluorocarbon oils against each other, is described. Using thaumatin as a test case at 1.8 Å resolution, this study demonstrates that high-resolution electron density maps and refined models can be obtained from in situ diffraction of crystals grown in microcapillaries.

SUBMITTER: Yadav MK

PROVIDER: S-EPMC1858637 | biostudies-literature | 2005 Dec

REPOSITORIES: biostudies-literature

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In situ data collection and structure refinement from microcapillary protein crystallization.

Yadav Maneesh K MK Gerdts Cory J CJ Sanishvili Ruslan R Smith Ward W WW Roach L Spencer LS Ismagilov Rustem F RF Kuhn Peter P Stevens Raymond C RC

Journal of applied crystallography 20051201 6

In situ X-ray data collection has the potential to eliminate the challenging task of mounting and cryocooling often fragile protein crystals, reducing a major bottleneck in the structure determination process. An apparatus used to grow protein crystals in capillaries and to compare the background X-ray scattering of the components, including thin-walled glass capillaries against Teflon, and various fluorocarbon oils against each other, is described. Using thaumatin as a test case at 1.8 Å resolu ...[more]

PMID: 17468785

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