Abstract
Dihydrofolate reductase (DHFR) from bacteriophage T4 is a homodimer consisting of 193-residue subunits. It has been crystallized in the presence of the cofactor (NADPH) and an inhibitor (aminopterin) at 296 K using sodium chloride as precipitant. The crystals are tetragonal, belonging to the space group P4(1)22 (or P4(3)22), with unit-cell parameters a = b = 61.14, c = 123.23 A under cryogenic conditions. The asymmetric unit contains a single subunit, with a corresponding V(m) of 2.65 A(3) Da(-1) and a solvent content of 53. 6%. Native data have been collected from a crystal to 1.9 A resolution using synchrotron X-rays.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacteriophage T4 / enzymology*
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Bacteriophage T4 / genetics*
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Crystallization
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Crystallography, X-Ray
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Data Collection
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Escherichia coli / virology
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Gene Expression Regulation, Bacterial
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Gene Expression Regulation, Viral
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Synchrotrons
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Tetrahydrofolate Dehydrogenase / biosynthesis
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Tetrahydrofolate Dehydrogenase / genetics*
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Tetrahydrofolate Dehydrogenase / isolation & purification
Substances
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Recombinant Proteins
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Tetrahydrofolate Dehydrogenase