Crystallization and preliminary diffraction studies of SFC-1, a carbapenemase conferring antibiotic resistance

SFC-1, a class A carbapenemase that confers antibiotic resistance, hydrolyzes the β-lactam rings of β-lactam antibiotics (carbapenems, cephalosporins, penicillins and aztreonam). SFC-1 presents an enormous challenge to infection control, particularly in the eradication of Gram-negative pathogens. As SFC-1 exhibits a remarkably broad substrate range, including β-lactams of all classes, the enzyme is a potential target for the development of antimicrobial agents against pathogens producing carbapenemases. In this study, SFC-1 was cloned, overexpressed, purified and crystallized. The SFC-1 crystal diffracted to 1.6 Å resolution and belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 65.8, b = 68.3, c = 88.8 Å. Two molecules are present in the asymmetric unit, with a corresponding V(M) of 1.99 Å(3) Da(-1) and a solvent content of 38.1%.