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

Bradley O. Elmore, Arwen R. Pearson, Carrie M. Wilmot, Alan B. Hooper

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

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 P31/221, with unit-cell parameters a = b = 53.3, c = 127.1 Å, and contain one monomer in the asymmetric unit.

Original languageEnglish (US)
Pages (from-to)395-398
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number4
DOIs
StatePublished - Apr 2006

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