Crystallization and preliminary crystallographic analysis of human serine dehydratase

Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2297-9. doi: 10.1107/s0907444903020110. Epub 2003 Nov 27.

Abstract

L-Serine dehydratase (SDH) catalyzes the pyridoxal phosphate (PLP) dependent deamination of L-serine to yield pyruvate. Recombinant human serine dehydratase was crystallized by the hanging-drop vapour-diffusion method. Crystals were grown at 291 K using (NH4)(2)SO4 as precipitant. Diffraction data were obtained to a resolution of 2.5 A from a single frozen crystal using Cu Kalpha radiation. The crystal belongs to space group I422, with unit-cell parameters a = 157.4, b = 157.4, c = 59.2 A, alpha = beta = gamma = 90 degrees. The asymmetric unit contains one molecule and has a solvent content of about 46%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization / methods
  • Crystallography, X-Ray / methods
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Humans
  • L-Serine Dehydratase / chemistry*
  • L-Serine Dehydratase / genetics
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics

Substances

  • Recombinant Proteins
  • L-Serine Dehydratase