Crystallization and preliminary crystallographic analysis of recombinant human calcyphosine

Protein Pept Lett. 2009;16(3):339-41. doi: 10.2174/092986609787601624.

Abstract

Human calcyphosine was cloned into the pET-28a vector and highly expressed in Escherichia coli BL21 (DE3) cells. The protein was purified and crystallized. The crystal diffracted to 2.8 A and belonged to space group P2(1)2(1)2, with the unit cell parameters a=70.39 A, b=132.02 A, c=46.20 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium-Binding Proteins / chemistry*
  • Calcium-Binding Proteins / genetics
  • Calcium-Binding Proteins / isolation & purification
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Humans
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification

Substances

  • CAPS protein, human
  • Calcium-Binding Proteins
  • Recombinant Proteins