title: Crystallization and synchrotron X-ray diffraction studies of human interleukin-22.
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.
authors.affiliation: Laboratório Nacional de Luz Síncrotron, Caixa Postal 6192, CEP 13083-970, Campinas, SP, Brazil.
authors.forename: R A P
authors.initials: RA
authors.lastname: Nagem
authors.forename: K W
authors.initials: KW
authors.lastname: Lucchesi
authors.forename: D
authors.initials: D
authors.lastname: Colau
authors.forename: L
authors.initials: L
authors.lastname: Dumoutier
authors.forename: J-C
authors.initials: JC
authors.lastname: Renauld
authors.forename: I
authors.initials: I
authors.lastname: Polikarpov
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D007378:Interleukins / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D000097043:Interleukin-22
chemical_list: D007378:Interleukins; D011994:Recombinant Proteins; D000097043:Interleukin-22