Purification, characterization, and crystallization of the adhesive domain of SdrD from Staphylococcus aureus.
The adhesive domain of SdrD from Staphylococcus aureus was solubly expressed in Escherichia coli in high yield. After a series of purification steps, the purified protein was >95% pure, which was SdrD from S. aureus identified by SDS-PAGE and MALDI-TOF MS. Crystals were grown at 18 degrees C using 25% polyethylene glycol 3350 as precipitant. Diffraction by the crystal extends to 1.65A resolution, and the crystal belongs to the space group C2, with the unit cell parameters a=133.3, b=58.3, c=112.3A, alpha=90.00, beta=111.14, gamma=90.00.
Zhang
Liqing
L
Department of Immunology, School of Basic Medical Sciences, Capital Medical University, Beijing 100069, People's Republic of China.
Xiang
Hua
H
Gao
Jinlan
J
Hu
Jia
J
Miao
Shiying
S
Wang
Linfang
L
Deng
Xuming
X
Li
Shentao
S
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003001:Cloning, Molecular; D003460:Crystallization; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013211:Staphylococcus aureus / Q000737:chemistry*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; C115915:SdrD protein, Staphylococcus aureus