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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.

Original publication

DOI

10.1107/S0907444904029567

Type

Journal article

Journal

Acta Crystallogr D Biol Crystallogr

Publication Date

02/2005

Volume

61

Pages

130 - 140

Keywords

Protein Conformation, Proteins, X-Ray Diffraction