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 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.
D000818:Animals; D003460:Crystallization; D003545:Cysteine / Q000032:analysis; D007370:Interferon Type I / Q000032:analysis; D051379:Mice; D011994:Recombinant Proteins / Q000032:analysis; D014961:X-Ray Diffraction
D007370:Interferon Type I; D011994:Recombinant Proteins; D003545:Cysteine