A clear narrative of complex structure determination, including crystallographic problems of pseudo-merohedral twinning, pseudo-translational symmetry and data anisotropy, is provided. This manuscript provides a description of how these issues encountered during the structural determination of E. coli type I pyruvate kinase to 2.28 Å resolution were overcome.

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 of N-acetylmannosamine kinase from methicillin-resistant S. aureus, a novel antibiotic target within sialic acid catabolism, 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.

Diaminopimelate decarboxylase catalyses the last step in lysine biosynthesis: the decarboxylation of meso-diaminopimelate to form the essential amino acid S-lysine. Here, the crystallization of the two putative diaminopimelate decarboxylase isoforms from Arabidopsis thaliana, DapDc1 and DapDc2, are reported; the crystals diffracted to beyond 2.00 and 2.27 Å resolution, respectively.