CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF BACTERIOPHAGE-T4 DEOXYNUCLEOTIDE KINASE

Citation
P. Sebastiao et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF BACTERIOPHAGE-T4 DEOXYNUCLEOTIDE KINASE, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 226-227
Citations number
13
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
ISSN journal
09074449
Volume
52
Year of publication
1996
Part
1
Pages
226 - 227
Database
ISI
SICI code
0907-4449(1996)52:<226:CAPAOB>2.0.ZU;2-0
Abstract
T4 deoxynucleotide kinase catalyzes the phosphorylation of 5-hydroxyme thyldeoxycytidylate, dTMP and dGMP while excluding dCMP and dAMP. In o rder to understand the mechanism of this remarkable specificity, the e nzyme was over-expressed in Escherichia coli, purified and crystallize d for X-ray diffraction analysis. The crystals belong to the monoclini c space group C2 with cell dimensions a = 155.2, b = 58.5, c = 75.7 An gstrom, beta = 108.1 degrees. There are two protein monomers in the as ymmetric unit related by a twofold axis. Diffraction data to 2.0 Angst rom resolution have been collected.