Crystallization and synchrotron X-ray diffraction studies of human interleukin-22

Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):529-30. doi: 10.1107/s0907444902001063. Epub 2002 Feb 21.

Abstract

Human interleukin-22, a novel member of the cytokine family, has been crystallized in hanging drops using the vapour-diffusion technique. Preliminary X-ray diffraction experiments using synchrotron radiation reveal that the protein crystallizes in space group P2(1)2(1)2(1), with unit-cell parameters a = 55.44, b = 61.62, c = 73.43 A, and diffracts beyond 2.00 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Interleukin-22
  • Interleukins / chemistry*
  • Protein Conformation
  • Recombinant Proteins / chemistry

Substances

  • Interleukins
  • Recombinant Proteins