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.