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Purification, crystallization, and preliminary X‐ray studies of 10‐formyltetrahydrofolate synthetase from Clostridia acidici‐urici
Author(s) -
D'Ari Linda,
Cheung Edwin,
Rabinowitz Jesse C.,
Bolduc Jill M.,
Huang JieYu,
Stoddard Barry L.
Publication year - 1997
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(199702)27:2<319::aid-prot18>3.0.co;2-p
Subject(s) - tetramer , crystallization , crystallography , enzyme , resolution (logic) , formate , chemistry , crystal (programming language) , stereochemistry , biochemistry , organic chemistry , artificial intelligence , computer science , catalysis , programming language
The 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 1 , with unit cell dimensions a = 102.4 Å b = 116.5 Å c = 115.8 Å and β = 103.5 Å. 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 3 /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. © 1997 Wiley‐Liss, Inc.