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Crystallization of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae (1996)

Monzingo, Arthur F. ; West, Mary G. ; Schelp, Elisabeth ; [et al.]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 26 (1996), S. 481-482

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ISSN: 0887-3585

Keywords: crystallization ; methylenetetrahydrofolate dehydrogenase ; eukaryotes ; prokaryotic enzymes ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: 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 P42212 with cell constants a = b = 75.9, c = 160.0 Å, and there is one 36 kDa molecule in the asymmetric unit. Crystals diffract to 2.9 Å resolution. Proteins 26:481-482 © 1996 Wiley-Liss, Inc.

Type of Medium: Electronic Resource

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