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Title
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Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement.
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Authors
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S.J.Smerdon,
T.J.Oldfield,
E.J.Dodson,
G.G.Dodson,
R.E.Hubbard,
A.J.Wilkinson.
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Ref.
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Acta Crystallogr B, 1990,
46,
370-377.
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PubMed id
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Abstract
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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.
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