The following articles are a selection of those recently accepted for publication in Acta Crystallographica Section F: Structural Biology Communications.
Crystallization of nepenthesin I using a low-pH crystallization screen
The aspartic protease from N. gracilis was crystallized in complex with the inhibitor pepstatin A using a newly formulated low-pH screen. X-ray diffraction data showed that the crystals diffracted to 2.8 Å resolution.
Structures of plasmepsin II from Plasmodium falciparum in complex with two hydroxyethylamine-based inhibitors
The crystal structures described here demonstrate the conformational flexibility of the active-site cavity of the plasmepsins. The interactions of the different moieties in the P1′ position of the inhibitors have to be taken into account in the design of new potent plasmepsin inhibitors.
Expression, purification, crystallization and X-ray diffraction analysis of ChiL, a chitinase from Chitiniphilus shinanonensis
The catalytic domain of ChiL, a chitinase from the chitin-degrading bacterium C. shinanonensis, was expressed, purified and crystallized. Preliminary X-ray analysis shows that the crystal belonged to the orthorhombic space group P212121 and diffracted to 1.25 Å resolution.
Crystallographic analysis of a cupin superfamily enzyme from Microcystis aeruginosa involved in aeruginosin biosynthesis
The recombinant expression, purification, crystallization and X-ray crystallographic analysis of AerE from M. aeruginosa, an enzyme belonging to the cupin superfamily which has been deduced to participate in the biosynthesis of the 2-carboxy-6-hydroxyoctahydroindole moiety of aeruginosin, are described.
addenda and errata