Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement
- 1 June 1990
- journal article
- Published by International Union of Crystallography (IUCr) in Acta crystallographica Section B, Structural science, crystal engineering and materials
- Vol. 46 (3) , 370-377
- https://doi.org/10.1107/s0108768189012450
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.Keywords
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