Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 10 (October 2005)

crystallization communications

Acta Cryst. (2005). F61, 892-894 [ doi:10.1107/S1744309105027752 ]

Purification, crystallization and initial X-ray crystallographic analysis of the putative GTPase PH0525 from Pyrococcus horikoshii OT3

N. K. Lokanath, H. Yamamoto, E. Matsunaga, M. Sugahara and N. Kunishima

Abstract: GTPases are involved in diverse cellular functions including cell proliferation, cytoskeleton organization and intracellular traffic. The putative GTPase PH0525 from Pyrococcus horikoshii OT3 has been overexpressed in Escherichia coli and purified. Two distinct crystal forms were grown by the microbatch method at 291 K using a very high protein concentration (80 mg ml^-1). Native data sets extending to resolutions of 2.3 and 2.4 Å have been collected and processed in space groups P2₁ and C222₁, respectively. Assuming the presence of one monomer per asymmetric unit gives V_M values of 2.6 and 2.4 Å³ Da^-1 for the P2₁ and C222₁ forms, respectively, which is consistent with dynamic light-scattering experiments, which show a monomeric state of the protein in solution.

Keywords: GTP-binding protein; guanosine triphosphatase; Pyrococcus horikoshii OT3.