Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to the extracellular IL-22R1 chain

Academic Article

Abstract

  • Interleukin-22 (IL-22) is a potent mediator of cellular inflammatory responses. Crystals of IL-22 bound to the extracellular high-affinity cell-surface receptor sIL-22R1 have been grown from polyethylene glycol solutions. Crystals suitable for X-ray diffraction analysis were only obtained with mutants of IL-22 and sIL-22R1 that removed the N-linked glycosylation sites found in the wild-type amino-acid sequences. The crystals belonged to space group P21, with unit-cell parameters a = 50.43, b = 76.33, c = 114.92 Å, β = 92.45°, and diffracted X-rays to 3.2 Å resolution. The crystallographic asymmetric unit contained two IL-22-sIL-22R1 complexes, corresponding to a solvent content of approximately 52%. © International Union of Crystallography 2008.
  • Digital Object Identifier (doi)

    Author List

  • Jones BC; Logsdon NJ; Walter MR
  • Start Page

  • 266
  • End Page

  • 269
  • Volume

  • 64
  • Issue

  • 4