| Literature DB >> 2231708 |
M Hennig1, B Schlesier, S Pfeffer, W E Höhne.
Abstract
A seed globulin from Vicia narbonensis L. has been crystallized by vapour diffusion induced pH-shift. Crystals are suitable for high-resolution X-ray structural analysis and diffract to better than 1.5 A. Narbonin crystallizes in the monoclinic space group P21 with alpha = 46.9 A, b = 75.5 A, c = 50.9 A, alpha = gamma = 90 degrees, beta = 120.5 degrees. The protein consists of one polypeptide chain that does not coincide with the subunits of legumin or vicilin after SDS/polyacrylamide gel electrophoresis and has a relative molecular mass of about 33,000.Entities:
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Year: 1990 PMID： 2231708 DOI： 10.1016/s0022-2836(05)80354-7
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469