title: Crystallization of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae.
abstract: Saccharomyces cerevisiae possesses three isozymes of 5,10-methylenetetrahydrofolate dehydrogenase (MTD). The NAD-dependent enzyme is the first monofunctional form found in eukaryotes. Here we report its crystallization in a form suitable for high-resolution structure. The space group is P4(2)2(1)2 with cell constants a = b = 75.9, c = 160.0 A, and there is one 36 kDa molecule in the asymmetric unit. Crystals diffract to 2.9 A resolution.
authors.affiliation: Department of Chemistry and Biochemistry, University of Texas at Austin 78712, USA.
authors.forename: A F
authors.initials: AF
authors.lastname: Monzingo
authors.forename: M G
authors.initials: MG
authors.lastname: West
authors.forename: E
authors.initials: E
authors.lastname: Schelp
authors.forename: D R
authors.initials: DR
authors.lastname: Appling
authors.forename: J D
authors.initials: JD
authors.lastname: Robertus
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D008754:Methylenetetrahydrofolate Dehydrogenase (NADP) / Q000737:chemistry*; D009243:NAD / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
chemical_list: D009243:NAD; D008754:Methylenetetrahydrofolate Dehydrogenase (NADP)