Open AccessA new method for predetermining the diffraction quality of protein crystals: using SOAP as a selection tool
Author(s) -
Owen Robin Leslie,
Garman Elspeth
Publication year - 2005
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904029567
Subject(s) - birefringence , diffraction , microscope , materials science , lysozyme , crystal (programming language) , protein crystallization , optical microscope , optics , quality (philosophy) , x ray crystallography , tenacity (mineralogy) , crystallography , chemistry , crystallization , scanning electron microscope , physics , computer science , composite material , biochemistry , organic chemistry , quantum mechanics , programming language
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.