In situ data collection and structure refinement from microcapillary protein crystallization

Year: 2005

Type: article

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.

Source: Journal of Applied Crystallography

DOI: 10.1107/s002188980502649x

Authors: Maneesh K. Yadav, Cory J. Gerdts, Ruslan Sanishvili, Ward W. Smith, L. Spencer Roach, Rustem F. Ismagilov, Peter Kuhn, Raymond C. Stevens

Institutions: Scripps Research Institute, University of Chicago, Argonne National Laboratory

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

Funders: U.S. Department of Energy, National Institutes of Health, Office of Science, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases, National Institute of Biomedical Imaging and Bioengineering, Basic Energy Sciences

OpenAlex ID: W2129848443