Lobster enolase crystallized by serendipity

Proteins. 1994 Apr;18(4):390-3. doi: 10.1002/prot.340180409.

Abstract

An unknown protein crystallized from a lobster muscle preparation in which arginine kinase was the majority component. It was identified as enolase by peptide sequencing and activity testing, and a SIRAS electron density map showed its three-dimensional structure to be very similar to that of yeast enolase.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine Kinase / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Muscles / enzymology*
  • Nephropidae / enzymology*
  • Phosphopyruvate Hydratase / chemistry
  • Phosphopyruvate Hydratase / isolation & purification*
  • Sequence Analysis
  • Sequence Homology, Amino Acid

Substances

  • Arginine Kinase
  • Phosphopyruvate Hydratase