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The structure of GlnK1, one of three GlnK proteins encoded by the hyperthermophilic archaeon A. fulgidus, was solved to 2.28 Å resolution.
The crystal structure of SMU.595, a putative dihydroorotate dehydrogenase (DHOD) from S. mutans, is reported at 2.4 Å resolution.
A crystal structure of the catalytic domain of glucoamylase from A. niger with Tris and glycerol bound in the active site has been solved by molecular replacement and refined to 1.9 Å resolution.
The structure of CP4, a haemopexin-fold protein from cow pea (Vigna unguiculata), has been determined at 2.1 Å resolution.
The crystal structure of an unliganded form of CTP synthase from S. solfataricus unambiguously establishes that while the active form of the enzyme is tetrameric, a dimeric form has been crystallized. A comparison with the tetrameric form of the E. coli enzyme suggests that rather large intramolecular movements accompany tetramerization.
The crystal structure of flap endonuclease 1 from the hyperthermophilic archaeon D. amylolyticus was determined at 2.00 Å resolution.
Enoyl-acyl carrier protein reductase (FabI) from P. aeruginosa was purified and crystallized. FabI was also cocrystallized with the inhibitor triclosan and the cofactor NADH. Crystals of native and complexed FabI diffracted to resolutions of 2.6 and 1.8 Å, respectively.
The expression, purification, crystallization and preliminary crystallographic analysis of recombinant β-mannanase from B. licheniformis strain DSM13 are described.
To gain insight into the structure of the IgCAM3 domain, the IgCAM3 domain of MLCK1 has been expressed, purified and crystallized.
The thermostable direct haemolysin from G. hollisae has been purified and crystallized in two crystal forms using the vapour-diffusion method.
A recombinant cysteine protease inhibitor from the human nematode parasite A. lumbricoides has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.1 Å resolution.
β-Transaminase from Mesorhizobium sp. strain LUK was crystallized. The crystals were found to belong to the orthorhombic space group C2221, with unit-cell parameters a = 90.91, b = 192.17, c = 52.75 Å. The crystals were obtained at 293 K and diffracted to a resolution of 2.5 Å.
Wild-type and H12A-mutant class II phospholipase D from L. intermedia venom were crystallized; the crystals diffracted to maximum resolutions of 1.95 and 1.60 Å, respectively.
This report describes the crystallization and preliminary structure determination of the TIR domain from a plant disease-resistance protein.
A disulfide cross-linked complex between bovine poly(A) polymerase and a chemically modified RNA was crystallized. X-ray diffraction data were collected to 2.25 Å resolution from crystals that belonged to space group P2.
The central plant immune regulator EDS1 (enhanced disease susceptibility1) from A. thaliana has been crystallized for the first time. Crystals of EDS1 in complex with its signalling partner SAG101 (senescence-associated gene101) diffracted to 3.5 Å resolution.
Piratoxin I, a noncatalytic and myotoxic Lys49-phospholipase A2 from B. pirajai venom, was cocrystallized with the inhibitor caffeic acid and a data set was collected to a resolution of 1.65 Å. The electron-density map unambiguously indicated that three inhibitor molecules interact with the C-terminus of the protein.
Crystals of the wild-type haloalkane dehalogenase DhaA derived from R. rhodochrous NCIMB 13064 and of its catalytically inactive variant DhaA13 were grown in the presence of various ligands and diffraction data were collected to high and atomic resolution.
Collection to 2.5 Å resolution of neutron diffraction data from crystals of the human ABO(H) blood group glycosyltransferase GTA, is presented with the preliminary joint refinement with the corresponding X-ray diffraction data.
Octaprenyl pyrophosphate synthase from H. pylori has been expressed, purified and crystallized, and a diffraction data set was collected to 2.00 Å resolution.
The crystallization of Lmo0540 from L. monocytogenes is reported.
Crystallization conditions are described for the cis- and trans-imide bond-containing SH2 domain of IL-2-inducible T-cell kinase.
The adhesin fimbriae-associated protein 1 (Fap1) is a surface protein of Streptococcus parasanguinis FW213 and plays a major role in the formation of dental plaque in humans. Here, the adhesive domain Fap1-NRα, which is activated by acidic pH, has been crystallized at pH 5.0 and diffraction data have been collected to 3.0 Å resolution.
The C-terminal domain of the DNA gyrase GyrA from S. aureus strain Mu50 was cloned, overexpressed, purified and crystallized. X-ray diffraction data were collected to a resolution of 2.80 Å.
The cytoplasmic domain of FlhB from A. aeolicus has been purified and crystallized.
A fungal family 11 endoxylanase has been crystallized at pH 8.5 and room-temperature X-ray and neutron diffraction data have been collected. Joint X-ray/neutron refinement is under way; the structural results will aid in rational engineering of the enzyme.
Phosphoribosylglycinamide formyltransferase (PurN) from Streptococcus mutans was expressed in E. coli, purified and studied crystallographically.
Intestinal fatty-acid binding proteins from human and rat have been crystallized in complex with the fluorescent probe 11-(dansylamino)undecanoic acid. Diffraction data for the crystals were collected to 1.8 Å resolution (human) and 1.6 Å resolution (rat).