Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):700-6. doi: 10.1107/S1744309108018757. Epub 2008 Jul 5.

Abstract

The decameric inducible lysine decarboxylase (LdcI) from Escherichia coli has been crystallized in space groups C2 and C222(1); the Ta6Br12(2+) cluster was used to derivatize the C2 crystals. The method of single isomorphous replacement with anomalous scattering (SIRAS) as implemented in SHELXD was used to solve the Ta6Br12(2+)-derivatized structure to 5 A resolution. Many of the Ta6Br12(2+)-binding sites had twofold and fivefold noncrystallographic symmetry. Taking advantage of this feature, phase modification was performed in DM. The electron-density map of LdcI displays many features in agreement with the low-resolution negative-stain electron-density map [Snider et al. (2006), J. Biol. Chem. 281, 1532-1546].

MeSH terms

  • Carboxy-Lyases / chemistry*
  • Carboxy-Lyases / genetics
  • Carboxy-Lyases / isolation & purification
  • Chromatography, Gel
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Protein Conformation

Substances

  • Carboxy-Lyases
  • lysine decarboxylase