ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006
Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea cytochrome, cytochrome P460.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- The Eponymous Cofactors in Cytochrome P460s from Ammonia-Oxidizing Bacteria Are Iron Porphyrinoids Whose Macrocycles Are Dibasic.Biochemistry · 2018Article
- Nitrosomonas europaea cytochrome P460 is a direct link between nitrification and nitrous oxide emission.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Is there a pathway for N2O production from hydroxylamine oxidoreductase in ammonia-oxidizing bacteria?Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The crystal structure of cytochrome P460 of Nitrosomonas europaea reveals a novel cytochrome fold and heme-protein cross-link.Biochemistry · 2007Article
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Authors and funding
4 authors.
Funding
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 angstroms 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 angstroms, and contain one monomer in the asymmetric unit.
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