title: Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement.
abstract: As part of a protein engineering study, the X-ray crystal structure of recombinant pig myoglobin, prepared and crystallized from E. coli, has been determined. Diffraction data were collected to 2.5 A spacing using a synchrotron X-ray source. The structure was solved using the molecular-replacement method and refined using least-squares minimization procedures to a crystallographic R factor of 18.5% using 14,481 reflections between 10 and 2.5 A. A preliminary comparison of the structure of pig myoglobin with other myoglobin structures is presented.
authors.affiliation: Department of Chemistry, University of York, Heslington, England.
authors.forename: S J
authors.initials: SJ
authors.lastname: Smerdon
authors.forename: T J
authors.initials: TJ
authors.lastname: Oldfield
authors.forename: E J
authors.initials: EJ
authors.lastname: Dodson
authors.forename: G G
authors.initials: GG
authors.lastname: Dodson
authors.forename: R E
authors.initials: RE
authors.lastname: Hubbard
authors.forename: A J
authors.initials: AJ
authors.lastname: Wilkinson
mesh_terms: D000818:Animals; D006418:Heme; D006860:Hydrogen Bonding; D016018:Least-Squares Analysis; D008722:Methods; D008958:Models, Molecular; D015394:Molecular Structure; D009211:Myoglobin; D011487:Protein Conformation; D011994:Recombinant Proteins; D012399:Rotation; D012984:Software; D013045:Species Specificity; D013552:Swine; D014907:Whales; D014961:X-Ray Diffraction
chemical_list: D009211:Myoglobin; D011994:Recombinant Proteins; D006418:Heme