Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12

Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):189-91. doi: 10.1107/s0907444999014936.

Abstract

S100A12, a member of the calgranulin family, isolated from human blood, has been crystallized by vapour diffusion in the presence of Ca(2+). Crystals belong to the space group R3 with unit-cell dimensions a = b = 99.6 c = 64.2 A. There are two monomers per asymmetric unit, with a solvent content of 57.9%. The crystals diffract to at least 2.2 A resolution and complete X-ray data have been collected to 2.5 A on a conventional laboratory source.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium-Binding Proteins / blood
  • Calcium-Binding Proteins / chemistry*
  • Calcium-Binding Proteins / physiology
  • Crystallization
  • Dimerization
  • Forecasting
  • Humans
  • Neutrophils / chemistry
  • S100 Proteins*
  • S100A12 Protein
  • Structure-Activity Relationship
  • X-Ray Diffraction

Substances

  • Calcium-Binding Proteins
  • S100 Proteins
  • S100A12 Protein
  • S100A12 protein, human