Enolase catalyzes the reversible conversion of 2-phosphoglycerate to phosphoenolpyruvate. Structural snapshots of Mycobacterium tuberculosis enolase provide critical insights into the mechanism of conversion of phosphoenolpyruvate to 2-phosphoglycerate.

The results of the fifth blind test of crystal structure prediction, which show important success with more challenging large and flexible molecules, are presented and discussed.

Cyclophin A like protein from Piriformospora indica involved in salt-stress tolerance was cloned, overexpressed, purified and crystallized. The crystals obtained diffracted X-rays to 2 Å resolution and belonged to space group C222₁.

The π-hole carbon bonding in a new hydrate cocrystal of gallic acid with pyrazine was characterized by static and dynamic charge density analysis.

The Escherichia coli PapD-like protein (EcpD), from uropathogenic Escherichia coli (UPEC), which is a periplasmic chaperon of Yad fimbriae was cloned, overexpressed, purified and crystallized. The crystals obtained diffracted X-rays to 1.67 Å resolution and belonged to space group C222₁.

L. donovani Rab5a (LdRab5a), a GTP-dependent molecular switch, regulates the fluid-phase endocytosis of essential nutrients. The crystal structure of the GTPase domain of LdRab5a has been determined in the GDP-bound form, which shows the canonical Rab fold but with a unique disposition of the Switch I region.