Crystallization and preliminary X-ray analysis of wild-type and K272A mutant glutamate 1-semialdehyde aminotransferase from Synechococcus

J Mol Biol. 1994 Sep 30;242(4):591-4. doi: 10.1006/jmbi.1994.1606.

Abstract

Crystals of the pyridoxal-5'-phosphate dependent enzyme glutamate-1-semialdehyde aminotransferase (EC 5.4.3.8) from Synechococcus have been grown from polyethylene glycol solutions. The wild-type enzyme crystallizes in space group P2(1)2(1)2(1), with cell dimensions a = 68.4 A, b = 108.0 A, c = 122.6 A. The inactive mutant in which the cofactor-binding lysine 272 residue is replaced by alanine (K272A) gives monoclinic crystals of space group P2(1) with cell dimensions a = 67.1 A, b = 108.6 A, c = 124.5 A and beta = 115.7 degrees. These crystal forms diffract to 2.4 A and 2.7 A resolution, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Cyanobacteria / enzymology*
  • Glutamates
  • Intramolecular Transferases*
  • Isomerases / chemistry*

Substances

  • Glutamates
  • glutamate-1-semialdehyde
  • Isomerases
  • Intramolecular Transferases
  • glutamate-1-semialdehyde 2,1-aminomutase