Crystal structure of Plasmodium falciparum proplasmepsin IV: the plasticity of proplasmepsins

The study of the crystal structure of proplasmepsin IV from P. falciparum and its comparison with the structures of the mature enzyme and of other proplasmepsins show the flexibility that characterizes the aspartic protease zymogens from malaria parasites.

A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis

The gene encoding a putative siderophore-interacting protein from the marine bacterium S. frigidimarina was successfully cloned, followed by expression and purification of the gene product. Optimized crystals diffracted to 1.35 Å resolution and preliminary crystallographic analysis is promising with respect to structure determination and increased insight into the poorly understood molecular mechanisms underlying iron acquisition.

pHluorin-assisted expression, purification, crystallization and X-ray diffraction data analysis of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I

The C-terminal domain of the HsdR subunit of the E. coli type I restriction-modification system EcoR124I was purified and crystallized in form of a pHluorin (GFP) fusion protein and X-ray diffraction data were collected to a resolution of 2.45 Å.

Surface-layer protein from Caulobacter crescentus: expression, purification and X-ray crystallographic analysis

The large C-terminal domain of the C. crescentus surface-layer protein RsaA has been crystallized. Initial RsaA crystals have been shown to diffract to ∼2.5 Å resolution.

The quorum-quenching lactonase from Geobacillus caldoxylosilyticus: purification, characterization, crystallization and crystallographic analysis

A lactonase, named GcL, from G. caldoxylosilyticus has been isolated, purified, characterized and crystallized. Here, it is shown that GcL is a thermostable enzyme that is extremely proficient at degrading lactones. Its structure is expected to provide insights regarding the catalytic mechanism and to highlight the structural determinants involved in the high proficiency of this enzyme.

Structural analysis of point mutations at the Vaccinia virus A20/D4 interface

The Vaccinia virus D4/A20 complex is the DNA polymerase cofactor. The heterodimer interface has been analysed using three new crystal structures of the complex in which key residues forming a cation–π interaction have been mutated.

Crystal structure of Halobacterium salinarum halorhodopsin with a partially depopulated primary chloride-binding site

A structure of halorhodopsin with about 50% occupancy of its primary chloride-binding site showed no structural changes in the protein, suggesting that anion binding is not strictly coupled to protein conformation in this crystal form.

Crystal structure of pyruvate de­carboxylase from Zymobacter palmae

The crystal structure of Z. palmae pyruvate decarboxylase was elucidated at 2.15 Å resolution.

The role of water molecules in the binding of class I and II peptides to the SH3 domain of the Fyn tyrosine kinase

The crystal structures of complexes of the SH3 domain of the Fyn tyrosine kinase with the high-affinity peptides VSL12 (class I) and APP12 (class II) have been solved at 1.6 and 2.1 Å resolution, respectively. These structures support an important role of water molecules in facilitating conformational changes to allow binding of the proline-rich motifs in the two available orientations in this family of SH3 domains.

Crystallization of and selenome­thionine phasing strategy for a SETMAR–DNA complex

The DNA-binding domain of SETMAR was successfully crystallized in a complex with its ancestral terminal inverted repeat and a variant of this sequence through a systematic approach, and initial Se SAD phasing was achieved through the judicious addition of Met residues.

Crystal structure of the YajQ-family protein XC_3703 from Xanthomonas campestris pv. campestris

The structure of XC_3703, a YajQ-family protein and a potential c-di-GMP receptor, has been determined at 2.1 Å resolution.

1.65 Å resolution structure of the AraC-family transcriptional activator ToxT from Vibrio cholerae

A crystal structure of ToxT at 1.65 Å resolution with a similar overall structure to the previously determined structure is reported. A region that extends from Asp101 to Glu110, which can influence ToxT activity but was disordered in the previous structure, can be traced entirely in the current structure.