Preliminary crystallographic investigations of glycinamide ribonucleotide transformylase.
Crystals of glycinamide ribonucleotide transformylase have been grown from 0.4 to 1 M ammonium sulfate, 0.6 to 1 M sodium-potassium phosphate, or 0.65 to 1 M citrate in the pH range 4.5-7.0. The single crystals display variable morphology with varying pH. The crystals belong to the orthorhombic space group C222 with cell dimensions a = 141.4 A, b = 98.2 A, c = 103.5 A. Co-crystals have also been obtained in the presence of the inhibitor 5,8-dideazafolate (KI = 18 microM) under similar crystallization conditions. Crystals of a chemically modified enzyme, iodinated at Cys-21, were grown under similar conditions within the pH range 6.5-7.0. These crystals are isomorphous with the unmodified enzyme. Crystals suitable for high resolution (less than 2.5 A) x-ray diffraction studies have been obtained for each of the above.
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Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.
Johnson
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Inglese
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Smith
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Benkovic
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Wilson
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D000217:Acyltransferases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D003461:Crystallography / Q000295:instrumentation / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology; D019877:Hydroxymethyl and Formyl Transferases; D051026:Phosphoribosylglycinamide Formyltransferase; D011487:Protein Conformation
D019877:Hydroxymethyl and Formyl Transferases; D051026:Phosphoribosylglycinamide Formyltransferase; D000217:Acyltransferases