Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 4 (April 2008)

crystallization communications

Acta Cryst. (2008). F64, 266-269 [ doi:10.1107/S1744309108004752 ]

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

B. C. Jones, N. J. Logsdon and M. R. Walter

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, [beta] = 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%.

Keywords: interleukin-22; sIL-22R1; cytokines.