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Crystals of cytochrome c‐553 from Bacillus pasteurii show diffraction to 0.97 å resolution
Author(s) -
Benini Stefano,
Ciurli Stefano,
Rypniewski Wojciech R.,
Wilson Keith S.
Publication year - 1997
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/(sici)1097-0134(199708)28:4<580::aid-prot11>3.0.co;2-c
Subject(s) - orthorhombic crystal system , crystallography , chemistry , cytochrome c , ammonium sulfate , crystal structure , organic chemistry , biochemistry , mitochondrion
We report here the purification and characterization of a c ‐type cytochrome present in the soluble fraction of the gram‐positive, alkaliphilic, and highly ureolytic soil bacterium Bacillus pasteurii. The cytochrome is acidic (pI = 3.3), has a molecular mass of 9.5 kDa, and appears to dimerize in 150 mM ionic strength solution. The electronic spectrum is typical of a low‐spin hexa‐coordinated heme iron. Crystals of the protein in the oxidized state were grown by vapor diffusion at pH 5, by using 3.2 M ammonium sulfate as precipitant. Diffraction data at ultrahigh resolution (0.97 Å) and completeness (99.9%) have been collected under cryogenic conditions, by using synchrotron radiation. The crystals belong to the orthorhombic space group P2 1 2 1 2 1 , with cell constants a = 37.14, b = 39.42, c = 44.02 Å, and one protein monomer per asymmetric unit. Attempts to solve the crystal structure by ab initio methods are in progress. Proteins 28:580–585, 1997 © 1997 Wiley‐Liss, Inc.