Preliminary crystallographic investigations of glycinamide ribonucleotide transformylase

J Biol Chem. 1989 Jun 5;264(16):9703-6.

Abstract

Crystals of glycinamide ribonucleotide transformylase have been grown from 0.4 to 1 M ammonium sulfate, 0.6 to 1 M sodium-potassium phosphate, or 0.65 to 1 M citrate in the pH range 4.5-7.0. The single crystals display variable morphology with varying pH. The crystals belong to the orthorhombic space group C222 with cell dimensions a = 141.4 A, b = 98.2 A, c = 103.5 A. Co-crystals have also been obtained in the presence of the inhibitor 5,8-dideazafolate (KI = 18 microM) under similar crystallization conditions. Crystals of a chemically modified enzyme, iodinated at Cys-21, were grown under similar conditions within the pH range 6.5-7.0. These crystals are isomorphous with the unmodified enzyme. Crystals suitable for high resolution (less than 2.5 A) x-ray diffraction studies have been obtained for each of the above.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acyltransferases / antagonists & inhibitors
  • Acyltransferases / isolation & purification*
  • Chemical Phenomena
  • Chemistry
  • Crystallography* / instrumentation
  • Crystallography* / methods
  • Escherichia coli / enzymology
  • Hydroxymethyl and Formyl Transferases*
  • Phosphoribosylglycinamide Formyltransferase
  • Protein Conformation

Substances

  • Hydroxymethyl and Formyl Transferases
  • Phosphoribosylglycinamide Formyltransferase
  • Acyltransferases