title: A new method for predetermining the diffraction quality of protein crystals: using SOAP as a selection tool.
abstract: 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.
authors.affiliation: Laboratory of Molecular Biophysics, Department of Biochemistry, Oxford University, Rex Richards Building, South Parks Road, Oxford OX1 3QU, England.
authors.forename: Robin Leslie
authors.initials: RL
authors.lastname: Owen
authors.forename: Elspeth
authors.initials: E
authors.lastname: Garman
mesh_terms: D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D011506:Proteins