N-Acetylneuraminate lyase, an enzyme involved in the bacterial uptake and metabolism of sialic acid, is a promising target for antibiotic development against pathogenic bacteria. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of N-acetylneuraminate lyase from methicillin-resistant S. aureus to 1.70 Å resolution are reported.

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis to 1.84 Å resolution of N-acetylmannosamine-6-phosphate 2-epimerase from methicillin-resistant S. aureus, an enzyme involved in the catabolism of sialic acid and a novel antimicrobial drug target, are reported.