Characterization, crystallization and preliminary X-ray analysis of the adhesive domain of SdrE from Staphylococcus aureus.
The adhesive domain of SdrE from Staphylococcus aureus was recombinantly expressed in Escherichia coli. The purified protein was identified by SDS-PAGE and MALDI-TOF MS. The protein was crystallized using the vapour-diffusion method in hanging-drop mode with PEG 8000 as the primary precipitating agent. X-ray diffraction data were collected to 1.8 A resolution from a single crystal of the protein. Preliminary X-ray analysis indicated that the crystal belonged to space group P1, with unit-cell parameters a = 40.714, b = 66.355, c = 80.827 A, alpha = 111.19, beta = 93.99, gamma = 104.39 degrees.
Xiang
Hua
H
Key Laboratory of Zoonosis, Ministry of Education, Institute of Zoonosis, College of Animal Science and Veterinary Medicine, Jilin University, Changchun 130062, People's Republic of China.
Gao
Fangfang
F
Wang
Dacheng
D
Liu
Jing
J
Hu
Jia
J
Zhang
Liqing
L
Li
Shentao
S
Deng
Xuming
X
D000268:Adhesiveness; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D013211:Staphylococcus aureus / Q000737:chemistry*
D001426:Bacterial Proteins; C118507:SdrE protein, Staphylococcus aureus