Crystallization and preliminary X-ray diffraction studies of a corrinoid protein from Sporomusa ovata

J Mol Biol. 1994 Feb 11;236(1):388-9. doi: 10.1006/jmbi.1994.1148.

Abstract

Crystals of a 40 kDa p-cresolyl-cobamide containing protein from Sporomusa ovata have been obtained from polyethyleneglycol solutions at pH 8.5 by the hanging drop technique. The crystals belong to space group C222(1) with cell dimensions a = 110.5(0.2) A, b = 144.0 (0.2) A, c = 110.4 (0.1) A. They diffract to 2.2 A resolution on a rotating anode X-ray source and are suitable for high resolution X-ray diffraction studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaea / chemistry*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Corrinoids
  • Crystallization
  • Crystallography, X-Ray / methods
  • Indicators and Reagents
  • Molecular Weight
  • Porphyrins / analysis*
  • Protein Conformation

Substances

  • Bacterial Proteins
  • Corrinoids
  • Indicators and Reagents
  • Porphyrins