The A component (SmhA) of a tripartite pore-forming toxin from Serratia marcescens: expression, purification and crystallographic analysis

SmhA, the A component of the tripartite α-pore-forming toxin from the opportunistic human pathogen Serratia marcescens, has been cloned, overexpressed and purified. Crystals were grown of selenomethionine-derivatized protein, anomalous data were collected, phases were calculated and an initial electron-density map was produced.

The X-ray crystal structure of the N-terminal domain of Ssr4, a Schizosaccharomyces pombe chromatin-remodelling protein

The N-terminal domain of Ssr4 from S. pombe, which is an integral protein in the SWI/SNF and RSC chromatin-remodelling complexes, has been crystallized and its structure has been solved using iodine as a phasing vehicle.

Crystal structure of barley agmatine coumaroyltransferase, an N-acyltransferase from the BAHD superfamily

The structure of barley agmatine coumaroyltransferase, a member of the BAHD acyltransferase superfamily, was elucidated. This is the first report of the structure of an N-acyltransferase from the BAHD superfamily.

The crystal structure of benzo­phenone synthase from Garcinia mangostana L. pericarps reveals the basis for substrate specificity and catalysis

The X-ray crystal structure of benzophenone synthase from G. mangostana L. reveals its active-site cavity and key residues catalyzing the conversion of its preferred substrate benzoyl-CoA to produce 2,4,6-trihydroxybenzophenone as the major product.

ATP-dependent RNA helicase domain of the ZC3H41 protein from Trypanosoma brucei: expression, purification and crystallization

In this study, a structural approach was used to unveil the molecular function of ZC3H41, an essential yet enigmatic protein in the life cycle of T. brucei. Here, the expression, purification and crystallization of this protein are reported.

The hypothetical periplasmic protein PA1624 from Pseudomonas aeruginosa folds into a unique two-domain structure

Crystal structure analysis of the hypothetical protein PA1624 from P. aeruginosa reveals a novel two-domain protein architecture that is only distantly reminiscent of previously characterized structural domains.

Computer-controlled liquid-nitrogen drizzling device for removing frost from cryopreserved crystals

Cryocrystallography, which is commonly used in macromolecular crystallography, may sometimes reduce the quality of diffraction data and the visibility of crystals owing to frost adhesion. A device has been developed to remove frost by drizzling liquid nitrogen over the crystals, which enabled noise reduction of diffraction images and the centering of crystals with low visibility owing to frost adhesion.

Crystallization of a nonclassical Kazal-type Carcinoscorpius rotundicauda serine protease inhibitor, CrSPI-1, complexed with subtilisin. Corrigendum

The article by Tulisas et al. [(2009), Acta Cryst. F65, 533–535] is corrected.