Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to the extracellular IL-22R1 chain
- 21 March 2008
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 64 (4) , 266-269
- https://doi.org/10.1107/s1744309108004752
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, = 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
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