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

Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):130-40. doi: 10.1107/S0907444904029567. Epub 2005 Jan 19.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Protein Conformation
  • Proteins / chemistry*
  • X-Ray Diffraction

Substances

  • Proteins