1pmb
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(New page: 200px<br /><applet load="1pmb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pmb, resolution 2.5Å" /> '''THE DETERMINATION OF ...)
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Revision as of 21:48, 20 November 2007
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THE DETERMINATION OF THE CRYSTAL STRUCTURE OF RECOMBINANT PIG MYOGLOBIN BY MOLECULAR REPLACEMENT AND ITS REFINEMENT
Overview
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.
About this Structure
1PMB is a Single protein structure of sequence from Sus scrofa with HEM as ligand. Full crystallographic information is available from OCA.
Reference
Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement., Smerdon SJ, Oldfield TJ, Dodson EJ, Dodson GG, Hubbard RE, Wilkinson AJ, Acta Crystallogr B. 1990 Jun 1;46 ( Pt 3):370-7. PMID:2383370
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