Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea cytochrome, cytochrome P460

被引:9
作者
Elmore, BO [1 ]
Pearson, AR [1 ]
Wilmot, CM [1 ]
Hooper, AB [1 ]
机构
[1] Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN 55455 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2006年 / 62卷
关键词
D O I
10.1107/S1744309106008785
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Cytochrome P460 from Nitrosomonas europaea, a novel mono-heme protein containing an unusual cross-link between a conserved lysine and the porphyrin ring, has been recombinantly expressed and purified from Escherichia coli. The protein crystallizes readily and diffraction to 1.7 angstrom has been obtained in-house. The crystals belong to the trigonal space group P3(1/2)21, with unit-cell parameters a = b = 53.3, c = 127.1 angstrom, and contain one monomer in the asymmetric unit.
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页码:395 / 398
页数:4
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