Sh. Sohn et al., Crystallization and preliminary X-ray crystallographic analysis of deoxycytidylate hydroxymethylase from bacteriophage T4, ACT CRYST D, 55, 1999, pp. 1061-1063
Deoxycytidylate hydroxymethylase from bacteriophage T4 is a homodimeric enz
yme in which each polypeptide chain consists of 246 amino-acid residues. It
has been crystallized in the presence of its substrate, deoxycytidine mono
phosphate, at room temperature using sodium citrate as precipitant. The cry
stals are monoclinic, belonging to space group C2, with unit-cell parameter
s a = 174.22, b = 53.12, c = 75.17 Angstrom, beta = 115.29 degrees. The asy
mmetric unit contains one homodimer, with a corresponding V-m of 2.65 Angst
rom(3) Da(-1) and solvent content of 54%. Native diffraction data to 1.6 An
gstrom resolution have been collected from two crystals using synchrotron r
adiation.