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The atomic resolution crystal structure of the double mutant (K53,56M) of bovine pancreatic phospholipase A2 is reported.
This article reports the production, crystallization and X-ray structure determination of perdeuterated human carbonic anhydrase (HCA II). The refined structure is shown to be highly isomorphous with hydrogenated HCA II, especially with regard to the active site architecture and solvent network.
Clitocypin is a cysteine protease inhibitor from the mushroom Clitocybe nebularis. The protein has been purified from natural sources and crystallized in a variety of non-isomorphous forms belonging to monoclinic and triclinic space groups.
X-ray crystallographic characterization of rhesus macaque MHC Mamu-A*02 complexed with an immunodominant SIV-Gag nonapeptide.
The olfactomedin (OLF) domain from the sea urchin cell-adhesion protein amassin has been crystallized. A native data set extending to 2.7 Å has been collected using an in-house X-ray source.
The endo-1,3-β-glucanase from alkaliphilic Nocardiopsis sp. strain F96 has been crystallized by the hanging-drop vapour-diffusion method. Diffraction data have been collected to 1.3 Å resolution.
The extracellular domain of the 4-1BB ligand fused with glutathione-S-transferase was expressed in Escherichia coli (Origami) and purified by using affinity and ion-exchange column chromatographic methods. Crystals of the 4-1BB ligand were obtained at 290 K by the hanging-drop vapour-diffusion method.
The arginine repressor of the hyperthermophile T. neapolitana was crystallized with and without its corepressor arginine. Both crystals diffracted to high resolution and belong to the orthorhombic space group P212121, with similar unit-cell parameters.
The tRNase domain of colicin D, which is specific to tRNAArgs, has been crystallized. A diffraction data set has been collected to a resolution of 1.05 Å.
A histidine acid phosphatase from the CDC Category A pathogen F. tularensis has been crystallized in space group P41212, with unit-cell parameters a = 61.96, c = 210.78 Å. A 1.75 Å resolution data set was collected at Advanced Light Source beamline 4.2.2.
Dihydropyrimidinase from the slime mould D. discoideum was crystallized. A single crystal was shown to belong to space group I222 and diffracted anisotropically to better than 1.8 Å.
Success in crystallization of a functionally intact Hsp70 chaperone required genetic engineering to minimize polydispersity and modulate interdomain interactions, as well as high concentrations of the potent structure stabilizer TMAO. These approaches may be generally useful in crystallization of conformationally flexible proteins that exhibit interdomain motions.
The GreB transcription cleavage factor of E. coli and the Gfh1 transcription elongation factor of T. thermophilus were cloned, expressed, purified and crystallized. Complete diffraction data sets were collected for the GreB and Gfh1 crystals to 2.6 and 2.8 Å resolution, respectively. Structure determination of these proteins is now in progress.
A putative ribosomal RNA-processing factor consisting of two KH domains from Pyrococcus horikoshii OT3 (PH1566; 25 kDa) was crystallized by the sitting-drop vapour-diffusion method using PEG 3000 as the precipitant. The space group of the crystals was determined as primitive orthorhombic P212121, with unit-cell parameters a = 45.9, b = 47.4, c = 95.7 Å.
MosA from S. meliloti L5-30 has been crystallized in solution with pyruvate and the 2.3 Å resolution structure has been solved by molecular replacement using E. coli dihydrodipicolinate synthase as the model.
Several crystals of the Grb2-like C-terminal SH3 domain in complex with a motif peptide from the SLP-76 protein were obtained and characterized.
The expression, purification, and crystallization in space group P212121 of the complex HasA-HasR from S. marcescens are reported. Diffraction data have been collected and processed to 6.8 Å.
Human RuvB-like protein RuvBL1 plays important roles in essential signaling pathways like c-Myc and Wnt, in transcription, and in DNA repair and apoptosis. Crystals of both native and a Se-Met derivative were obtained and characterized. SAD data leading to the structure solution at 2.2 Å were measured from the Se-Met crystals.
The purification, detergent-exchange protocol and crystallization conditions that led to the discovery of HPBP are reported. HPBP is a new human apoprotein that is absent from the genomic database and is the first phosphate transporter characterized in human plasma.
X-ray diffraction data were collected to 1.9 Å from crystals of HLA-G. Cobalt ions were found to be essential for the production of diffracting crystals.
The P. rubrum sucrose isomerase SmuA, a key enzyme in the industrial production of isomaltulose, was crystallized and diffraction data were collected to 1.95 Å resolution.
Monoclinic (P21) crystals of a His-tagged form of V. salmonicida catalase without cofactor diffract X-rays to 1.96 Å.
Human common-type acylphosphatase was crystallized in space group P212121, with unit-cell parameters a = 42.58, b = 47.23, c = 57.26 Å. A complete diffraction data set was collected to 1.45 Å.