Crystallization of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase fromSaccharomyces cerevisiae

✍ Scribed by Monzingo, Arthur F.; West, Mary G.; Schelp, Elisabeth; Appling, Dean R.; Robertus, Jon D.

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 189 KB
• Volume: 26
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(199612)26:4<481::aid-prot10>3.0.co;2-j

✦ Synopsis

Saccharomyces

cerevisiae possesses three isozymes of 5,lO-methylenetetrahydrofolate dehydrogenase (MTD). The NADdependent 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 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. Proteins 26481-482 @ 1996 Wiley-Liss, Inc.