Crystallization and preliminary crystallographic studies of human septin 1 with site-directed mutations.
Septin 1 is a member of an evolutionarily conserved family of GTP-binding and filament-forming proteins named septins, which function in diverse processes including cytokinasis, vesicle trafficking, apoptosis, remodelling of the cytoskeleton, infection, neurodegeneration and neoplasia. Human septin 1 has been expressed and purified, but suffers from severe aggregation. Studies have shown that septin 1 with site-directed mutations of five serine residues (Ser19, Ser206, Ser307, Ser312 and Ser315) has a much lower degree of aggregation and better structural homogeneity and that the mutations cause only slight perturbations in the secondary structure of septin 1. This septin 1 mutant was crystallized and diffraction data were collected to 2.5 A resolution. The space group is P422, with unit-cell parameters a = b = 106.028, c = 137.852 A.
Hu
Hao
H
Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Yu
Wen-bo
WB
Li
Shu-xing
SX
Ding
Xiang-ming
XM
Yu
Long
L
Bi
Ru-Chang
RC
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D016297:Mutagenesis, Site-Directed; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000235:genetics*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012694:Serine / Q000235:genetics
D011994:Recombinant Proteins; D012694:Serine; D010744:Phosphoric Monoester Hydrolases