Crystallization and preliminary crystallographic study of human CksHs1: a cell cycle regulatory protein.
The cell cycle regulatory protein CksHs1 has been crystallized in a form suitable for X-ray studies. CksHs1 crystals were grown in the presence of vanadate, a phosphatase inhibitor, but were also obtained with phosphate or tungstate as a cofactor. They belong to the hexagonal space group P6(1)22 with unit cell dimensions: a = b = 94 A, c = 131.6 A, and gamma = 120 degrees. The crystals grown in the presence of vanadate diffract X-rays to at least 2.8 A. Molecular replacement results from the homologous human CksHs2 structure reveal that a dimer forms the crystal habit, giving the unusual Vm value of 4.4 A3/Da or a solvent content of 72%.
Arvai
A S
AS
Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.
Bourne
Y
Y
Williams
D
D
Reed
S I
SI
Tainer
J A
JA
D042846:CDC2-CDC28 Kinases; D002352:Carrier Proteins / Q000737:chemistry*; D018797:Cell Cycle Proteins / Q000737:chemistry*; D003460:Crystallization; D003461:Crystallography; D018844:Cyclin-Dependent Kinases; D006801:Humans; D008958:Models, Molecular; D011494:Protein Kinases; D014961:X-Ray Diffraction
C093090:CKS1B protein, human; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D011494:Protein Kinases; D042846:CDC2-CDC28 Kinases; D018844:Cyclin-Dependent Kinases