Crystallization and preliminary X-ray analysis of Sau3AI C-terminal 232-419 amino acids fragment.
The C-terminal 232-419 amino acids fragment of endonuclease Sau3AI has been successfully expressed in Escherichia coli with 6 His at its N-terminal. After purification and crystallization, one completed 2.8 A data set was collected using a Rigaku R-AXIS IV++ diffractometer. The plate-like crystals belong to orthorhombic space group P2(1)2(1)2(1) with the cell dimension of a = 34.75, b = 76.82, c = 123.59A and contain one molecule per asymmetric unit.
Yu
Feng
F
Shanghai Institutes of Applied Physics, Chinese Academy of Sciences, Shanghai, China.
Song
Jiaping
J
Xu
Chunyan
C
Ding
Yu
Y
Hu
Xiaojian
X
He
Jianhua
J
Zhang
Zhihong
Z
D000596:Amino Acids / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015252:Deoxyribonucleases, Type II Site-Specific / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D013211:Staphylococcus aureus / Q000201:enzymology*
D000596:Amino Acids; D010446:Peptide Fragments; D015252:Deoxyribonucleases, Type II Site-Specific; C024405:GATC-specific type II deoxyribonucleases