N. Sakai et al., The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: crystallization and preliminary X-ray analysis, ACT CRYST D, 57, 2001, pp. 896-897
MinD is one of the proteins regulating cell division. MinD from Escherichia
coli has been designated as a type of motor protein which has an ATPase ac
tivity. This paper deals with the first crystallization and preliminary cry
stallographic analysis of recombinant MinD from Pyrococcus horikoshii (mole
cular weight 26.3 kDa) expressed in E. coli. Crystals of MinD were obtained
by the hanging-drop vapour-iffusion method. MinD crystals belong to space
group P2(1)3, with unit-cell parameters a = b = c = 98.5 Angstrom, and diff
ract to 3.0 Angstrom resolution. The asymmetric units each contain one mole
cule of MinD, giving a crystal volume per protein mass (VM) of 3.0 Angstrom
(3) Da(-1) and a solvent content of 59.0%.