Crystallization and preliminary X-ray studies of recombinant murine interferon-beta

Recombinant murine interferon-beta produced in Escherichia coli was purified and crystallized in an orthorhombic space group C222(1) with a = 61.67 A, b = 55.62 A, and c = 92.16 A. The crystals with a slight tendency for orientational disorder around the c axis diffract at least up to 3.3-A resoluti...

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Bibliographic Details
Published in:The Journal of biological chemistry 1986-12, Vol.261 (34), p.16207-16209
Main Authors: Matsuda, S, Kawano, G, Itoh, S, Mitsui, Y, Iitaka, Y
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Crystallization
Cysteine - analysis
Fundamental and applied biological sciences. Psychology
Holoproteins
Interferon Type I - analysis
Mice
Other proteins
Proteins
Recombinant Proteins - analysis
X-Ray Diffraction
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Summary:Recombinant murine interferon-beta produced in Escherichia coli was purified and crystallized in an orthorhombic space group C222(1) with a = 61.67 A, b = 55.62 A, and c = 92.16 A. The crystals with a slight tendency for orientational disorder around the c axis diffract at least up to 3.3-A resolution. The crystallizability and the fact that the crystallographic asymmetric unit contains only one molecule of murine interferon-beta strongly indicate that the present preparation (Matsuda, S., Utsumi, J., and Kawano, G. (1986) J. Interferon Res., in press) of recombinant murine interferon-beta is predominantly homogeneous with respect to chemical, tertiary, and quaternary structures.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)66699-2