Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea cytochrome, cytochrome P460.
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.
Department of Biochemistry, Molecular Biology and Biophysics, The University of Minnesota, Minneapolis, Minnesota, USA.
Bradley O
BO
Elmore
Arwen R
AR
Pearson
Carrie M
CM
Wilmot
Alan B
AB
Hooper
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D017124:Conserved Sequence; D003460:Crystallization; D003580:Cytochromes / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D017931:DNA Primers; D006420:Hemeproteins / Q000737:chemistry; D008239:Lysine; D013058:Mass Spectrometry; D043370:Nitrosomonas europaea / Q000201:enzymology*; D016133:Polymerase Chain Reaction; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D003580:Cytochromes; D017931:DNA Primers; D006420:Hemeproteins; C080650:cytochrome P-460; D008239:Lysine