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Purification, crystallization, and preliminary X-ray studies of 10- formyltetrahydrofolate synthetase from Clostridia acidici-urici
D'Ari L.; Cheung E.; Rabinowitz J.C.; Bolduc J.M.; Huang J.-Y.; Stoddard B.L.
1997-03-22
Source PublicationProteins: Structure, Function and Genetics
ISSN08873585
Volume27Issue:2Pages:319-321
AbstractThe monofunctional enzyme 10-formyltetrahydrofolate synthetase (THFS), which is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways, has been subcloned, purified, and crystallized. The crystals belong to space group P2, with unit cell dimensions a = 102.4 Å, b = 116.5 Å, c = 115.8 Å, and β = 103.5. The crystal unit cell and diffraction is consistent with an asymmetric unit consisting of the enzyme tetramer, and a specific volume of the unit cell of 2.7 Å/Da. The crystals diffract to at least 2.3 Å resolution after flash-cooling, when using a rotating anode x-ray source and an RAXIS image plate detector.
Keywordfolate coenzymes protein crystallization purine synthesis tetrahydrofolate
DOI10.1002/(SICI)1097-0134(199702)27:2<319::AID-PROT18>3.0.CO;2-P
URLView the original
Language英語
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Document TypeJournal article
专题University of Macau
AffiliationFred Hutchinson Cancer Research Center
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D'Ari L.,Cheung E.,Rabinowitz J.C.,et al. Purification, crystallization, and preliminary X-ray studies of 10- formyltetrahydrofolate synthetase from Clostridia acidici-urici[J]. Proteins: Structure, Function and Genetics,1997,27(2):319-321.
APA D'Ari L.,Cheung E.,Rabinowitz J.C.,Bolduc J.M.,Huang J.-Y.,&Stoddard B.L..(1997).Purification, crystallization, and preliminary X-ray studies of 10- formyltetrahydrofolate synthetase from Clostridia acidici-urici.Proteins: Structure, Function and Genetics,27(2),319-321.
MLA D'Ari L.,et al."Purification, crystallization, and preliminary X-ray studies of 10- formyltetrahydrofolate synthetase from Clostridia acidici-urici".Proteins: Structure, Function and Genetics 27.2(1997):319-321.
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