화학공학소재연구정보센터
Protein Expression and Purification, Vol.69, No.2, 204-208, 2010
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 1.65 angstrom resolution, and the crystal belongs to the space group C2, with the unit cell parameters a = 133.3, b = 58.3, c = 112.3 angstrom, alpha = 90.00, beta = 111.14, gamma = 90.00. (C) 2009 Elsevier Inc. All rights reserved.