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