A new method for predetermining the diffraction quality of protein crystals: using SOAP as a selection tool.

Autor: Owen RL; Laboratory of Molecular Biophysics, Department of Biochemistry, Oxford University, Rex Richards Building, South Parks Road, Oxford OX1 3QU, England., Garman E
Jazyk: angličtina
Zdroj: Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2005 Feb; Vol. 61 (Pt 2), pp. 130-40. Date of Electronic Publication: 2005 Jan 19.
DOI: 10.1107/S0907444904029567
Abstrakt: A microscope for quantitative analysis of the birefringence properties of samples is introduced. The microscope is used to measure variations in the slow optical axis position (SOAP) across hen egg-white lysozyme, glucose isomerase and fibronectin crystals. By comparing these variations with indicators of diffraction quality, it is shown that the optical properties of a protein crystal provide a non-invasive method of determining crystal diffraction quality before any X-ray data collection is attempted.
Databáze: MEDLINE