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

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

Authors :
Elmore, Bradley O.
Pearson, Arwen R.
Wilmot, Carrie M.
Hooper, Alan B.
Source :
Acta Crystallographica: Section F (Wiley-Blackwell); Apr2006, Vol. 62 Issue 4, p395-398, 4p, 1 Color Photograph, 1 Black and White Photograph, 1 Diagram, 1 Chart
Publication Year :
2006

Abstract

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 Å has been obtained in-house. The crystals belong to the trigonal space group P3<subscript>1/2</subscript>21, with unit-cell parameters a = b = 53.3, c = 127.1 Å, and contain one monomer in the asymmetric unit. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
62
Issue :
4
Database :
Complementary Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
20386443
Full Text :
https://doi.org/10.1107/S1744309106008785