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
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism
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Base Sequence
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Cloning, Molecular
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Conserved Sequence
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Crystallization
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Cytochromes / chemistry*
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Cytochromes / genetics
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Cytochromes / isolation & purification
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Cytochromes / metabolism
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DNA Primers
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Hemeproteins / chemistry
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Lysine
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Mass Spectrometry
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Nitrosomonas europaea / enzymology*
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Polymerase Chain Reaction
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X-Ray Diffraction
Substances
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Bacterial Proteins
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Cytochromes
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DNA Primers
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Hemeproteins
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cytochrome P-460
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Lysine