The cholesterol-dependent cytolysin listeriolysin O from L. monocytogenes has been purified and crystallized. The orthorhombic crystals diffracted to beyond 2.2 Å resolution and contained one molecule in the asymmetric unit.
The cloning, purification, crystallization and preliminary X-ray diffraction studies of S. aureus homoserine dehydrogenase, an enzyme that regulates the biosynthesis of several essential amino acids, are reported.
The globular cargo-binding domain of human Myo5a was cloned, expressed, purified and crystallized and the crystals were characterized. Special precautions that were necessary to harvest diffraction-quality crystals are described.
A phosphotriesterase-like lactonase dubbed VmoLac isolated from the hyperthermophilic crenarchaeon V. moutnovskia was purified and crystallized. A diffraction data set was collected to 2.4 Å resolution.
spMCAT from Synechocystis sp. PCC 6803, the first MCAT counterpart from a cyanobacterium, has been successfully cloned, purified and crystallized. A high-quality crystal with good diffraction has been obtained.
The CIDE-N domain of CIDE-3 was purified and crystallized. The crystals were found to belong to space group P32, with unit-cell parameters a = b = 63.35, c = 37.60 Å, γ = 120°. The crystals were obtained at 293 K and diffracted to a resolution of 2.0 Å.
Profilin from the helminthic parasite S. japonicum was expressed, purified and crystallized. The protein was found to be folded and to possess the expected secondary-structure content as determined by circular-dichroism spectroscopy.
MJ0458 protein, an adenylate kinase from Methanocaldococcus jannaschii which is a rich resource of unique enzymes, was crystallized and a set of X-ray diffraction data to 2.70 Å resolution was collected on the beamline BL-17U of the Shanghai Synchrotron Radiation Facility (SSRF). The crystal belonged to space group P41212 or P43212. The unit-cell parameters were a = b = 76.18, c = 238.70 Å, α = β = γ = 90°.
To investigate the molecular basis of immune signalling initiated by the TIR domains of plant disease-resistance proteins, the crystallization and preliminary X-ray diffraction analyses of the TIR domains of three proteins involved in disease resistance in A. thaliana are reported.
The C-terminal coiled-coil domain of SCP3, which is part of the lateral element of the synaptonemal complex, was purified and crystallized. The crystals were found to belong to space group C2, with unit-cell parameters a = 121.29, b = 43.08, c = 57.42 Å, β = 100.71°. The crystals were obtained at 293 K and diffracted to a resolution of 3.2 Å.
The reduced form of the terminal oxygenase component of carbazole 1,9a-dioxygenase from Janthinobacterium sp. J3 was crystallized. The crystals belonged to space group P65 and diffracted to 1.74 Å resolution.
Crystallization and preliminary X-ray studies of a ternary complex consisting of the ribosomal protein L11, the two-domain N-terminal fragment of the ribosomal protein P0 and a specific fragment of 23S rRNA from the archaeon M. jannaschii are reported.
The crystallization and preliminary crystallographic analysis of the putative NlpC/P60 endopeptidase, TTHA0266 is reported. The crystal belonged to space group P61 and the structure was solved with the single-wavelength anomalous dispersion method.