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Crystallization of the NAD‐dependent 5,10‐methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae
Author(s) -
Monzingo Arthur F.,
West Mary G.,
Schelp Elisabeth,
Appling Dean R.,
Robertus Jon D.
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199612)26:4<481::aid-prot10>3.0.co;2-j
Subject(s) - crystallization , nad+ kinase , dehydrogenase , saccharomyces cerevisiae , resolution (logic) , enzyme , chemistry , isozyme , crystallography , biochemistry , stereochemistry , yeast , organic chemistry , artificial intelligence , computer science
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 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.