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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt 4):395-8. doi: 10.1107/S1744309106008785. Epub 2006 Mar 25.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Cloning, Molecular
  • Conserved Sequence
  • Crystallization
  • Cytochromes / chemistry*
  • Cytochromes / genetics
  • Cytochromes / isolation & purification
  • Cytochromes / metabolism
  • DNA Primers
  • Hemeproteins / chemistry
  • Lysine
  • Mass Spectrometry
  • Nitrosomonas europaea / enzymology*
  • Polymerase Chain Reaction
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Cytochromes
  • DNA Primers
  • Hemeproteins
  • cytochrome P-460
  • Lysine