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Updated: Aug 9, 2026
Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea
Bradley O Elmore1, Arwen R Pearson, Carrie M Wilmot
1Department of Biochemistry, Molecular Biology and Biophysics, The University of Minnesota, Minneapolis, Minnesota, USA.
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.
