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Crystallization and preliminary X-ray diffraction study of a protein with a high potential rubredoxin center and a hemerythrin-type Fe center

✍ Scribed by L. C. Sieker; S. Turley; B. C. Prickril; J. LeGall

Publisher: John Wiley and Sons
Year: 1988
Tongue: English
Weight: 294 KB
Volume: 3
Category: Article
ISSN: 0887-3585
DOI: 10.1002/prot.340030306

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✦ Synopsis

A newly discovered iron-containing protein, isolated from the bacterium Desulfovibrio vulgaris (Hildenborough, NCIB 8303), has been crystallized. The molecule appears to be a dimer of mass 44kDa. This protein has iron centers with spectrascopic similarities to those in rubredoxins and in hemerythrins. The X-ray diffraction shows symmetry consistent with space group I222 or I212121. Cell parameters are a = 49.2 A, b = 81.3 A, c = 100.1 A, and alpha, beta, gamma = 90 degrees. X-ray diffraction data have been collected to 3.0 A, and a search for useful heavy atom derivatives is in progress for the analysis of the crystal structure of this Fe-protein.

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