Premium
Crystallization and preliminary X‐ray diffraction study of a protein with a high potential rubredoxin center and a hemerythrin‐type Fe center
Author(s) -
Sieker L. C.,
Turley S.,
Prickril B. C.,
LeGall J.
Publication year - 1988
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340030306
Subject(s) - rubredoxin , desulfovibrio vulgaris , crystallography , crystallization , dimer , x ray crystallography , chemistry , diffraction , protein crystallization , molecule , center (category theory) , bacteria , physics , biology , genetics , organic chemistry , optics
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 spectroscopic similarities to those in rubredoxins and in hemerythrins. The X‐ray diffraction shows symmetry consistent with space group I222 or I2 1 2 1 2 1 . Cell parameters are a = 49.2 Å, b = 81.3 Å, c= 100.1 Å, and α, β, γ = 90°. X‐ray diffraction data have been collected to 3.0 Å, and a search for useful heavy atom derivatives is in progress for the analysis of the crystal structure of this Fe‐protein.