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
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.