Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement.
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.
Smerdon
S J
SJ
Department of Chemistry, University of York, Heslington, England.
Oldfield
T J
TJ
Dodson
E J
EJ
Dodson
G G
GG
Hubbard
R E
RE
Wilkinson
A J
AJ
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
D009211:Myoglobin; D011994:Recombinant Proteins; D006418:Heme