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Digitale Medien

Crystallization and preliminary X-ray investigation of recombinant human interleukin 10 (1995)

Cook, William J. ; Windsor, William T. ; Murgolo, Nicholas J. ; [weitere]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 22 (1995), S. 187-190

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ISSN: 0887-3585

Schlagwort(e): cytokine ; BCRF1 ; protein structure ; crystal seeding ; Chemistry ; Biochemistry and Biotechnology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Medizin

Notizen: Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P41212 or P43212; the unit cell axes are a = 36.5 Å and c = 221.9 Å. There is the equivalent of one polypeptide chain in the asymmetric unit. The crystals are stable to X-rays and diffract to at least 2.5 Å resolution. © 1995 Wiley-Liss, Inc.

Zusätzliches Material: 1 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/prot.340220211

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Digitale Medien

Purification and crystallization of a complex between human interferon γ receptor (extracellular domain) and human interferon γ (1996)

Windsor, William T. ; Walter, Leigh J. ; Syto, Rosalinda ; [weitere]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 26 (1996), S. 108-114

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ISSN: 0887-3585

Schlagwort(e): crystallization ; interferon-γ ; receptor complex ; purification ; Chemistry ; Biochemistry and Biotechnology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Medizin

Notizen: X-ray diffraction quality crystals have been obtained from a complex between interferon γ and the extracellular domain of its high-affinity cell surface receptor. The crystals were obtained from interferon γ/interferon γ receptor complexes purified by size exclusion chromatography. Diffraction quality crystals required analyzing these complex samples by isoelectric focusing gels to select purified complex fractions devoid of unbound interferon γ. These studies used interferon γ receptor engineered with an eight amino acid N-terminal deletion to eliminate heterogeneity generated due to proteolytic cleavage. In addition, the receptor was expressed in an E. coli secretion cell line which eliminated the need to refold the protein. Hexagonal crystals were grown from 1.6 M ammonium phosphate solutions and belong to a spacegroup of P6522 with unit cell dimensions a = 145.9 Å and c = 180.3 Å. These crystals diffract to at least 2.9 Å resolution when exposed to synchrotron radiation. SDS PAGE analysis of the crystals demonstrated that both interferon γ and the receptor were present. Analysis of the x-ray diffraction data revealed that the crystals contain complexes with a stoichiometry of 2:1 receptor: ligand within the crystallographic asymmetric unit and consist of approximately 55% solvent. © 1996 Wiley-Liss, Inc.

Zusätzliches Material: 5 Ill.

Materialart: Digitale Medien

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