| Literature DB >> 19766722 |
Liqing Zhang1, Hua Xiang, Jinlan Gao, Jia Hu, Shiying Miao, Linfang Wang, Xuming Deng, Shentao Li.
Abstract
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.Entities:
Mesh：
Substances：
Year: 2009 PMID： 19766722 DOI： 10.1016/j.pep.2009.09.007
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650