

Publisher: John Wiley & Sons Inc
E-ISSN: 1744-3091|68|9|1124-1127
ISSN: 1744-3091
Source: Acta Crystallographica Section F, Vol.68, Iss.9, 2012-09, pp. : 1124-1127
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Abstract
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 P212121, 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 VM of 1.99 Å3 Da−1 and a solvent content of 38.1%.
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