Vcn. Yim et al., Crystallization and preliminary X-ray diffraction studies of glycerol 3-phosphate cytidylyltransferase from Staphylococcus aureus, ACT CRYST D, 57, 2001, pp. 918-920
Glycerol 3-phosphate cytidylyltransferase from Staphylococcus aureus (TarD(
Sa)) has been expressed in Escherichia coli, purified to homogeneity and cr
ystallized. The strategy used for determining crystallization conditions em
ployed hanging-drop sparse-matrix screens and required a combination of thr
ee different optimization approaches. Specifically, the presence or absence
of cofactors needed to be surveyed, the effects of small-molecule additive
s required exploration and the rate of vapour-diffusion had to be varied in
order to obtain crystals of TarD(Sa) suitable for diffraction studies. Cry
stals thus obtained belong to the space group P3(1)21, with unit-cell param
eters a = b = 92.2, c = 156.1 Angstrom, and contain four TarD(Sa) molecules
per asymmetric unit. The resolution limit observed for these crystals usin
g synchrotron radiation is 3.0 Angstrom.