Purification, crystallization and initial X-ray crystallographic analysis of the putative GTPase PH0525 from Pyrococcus horikoshii OT3
Journal Article
·
· Acta Crystallographica. Section F
- Advanced Protein Crystallography Research Group, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148 (Japan)
The putative GTPase PH0525 from P. horikoshii OT3 was crystallized using the microbatch method. Crystals were formed under two different conditions, providing two distinct crystal forms. Diffraction data from the two forms were measured to resolution limits of 2.30 and 2.40 Å and processed in space groups P2{sub 1} and C222{sub 1}, respectively. 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{sup −1}). Native data sets extending to resolutions of 2.3 and 2.4 Å have been collected and processed in space groups P2{sub 1} and C222{sub 1}, respectively. Assuming the presence of one monomer per asymmetric unit gives V{sub M} values of 2.6 and 2.4 Å{sup 3} Da{sup −1} for the P2{sub 1} and C222{sub 1} forms, respectively, which is consistent with dynamic light-scattering experiments, which show a monomeric state of the protein in solution.
- OSTI ID:
- 22356217
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 10 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Purification, crystallization and preliminary crystallographic analysis of the putative thiamine-biosynthesis protein PH1313 from Pyrococcus horikoshii OT3
Purification, crystallization and preliminary X-ray diffraction studies of a putative UDP-N-acetyl-d-mannosamine dehydrogenase from Pyrococcus horikoshii OT3
Crystallization and preliminary X-ray analysis of PH1566, a putative ribosomal RNA-processing factor from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
Journal Article
·
Sun Dec 31 23:00:00 EST 2006
· Acta Crystallographica. Section F
·
OSTI ID:22360252
Purification, crystallization and preliminary X-ray diffraction studies of a putative UDP-N-acetyl-d-mannosamine dehydrogenase from Pyrococcus horikoshii OT3
Journal Article
·
Tue May 01 00:00:00 EDT 2007
· Acta Crystallographica. Section F
·
OSTI ID:22360318
Crystallization and preliminary X-ray analysis of PH1566, a putative ribosomal RNA-processing factor from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
Journal Article
·
Sat Dec 31 23:00:00 EST 2005
· Acta Crystallographica. Section F
·
OSTI ID:22356251