|Home | About | Journals | Submit | Contact Us | Français|
The X-ray structure of a fungal lysozyme shows a modified α/β-barrel-like fold and a likely active-site DXE motif.
The first structure of a 14-3-3 protein–phosphopeptide complex is reported at 1.15 Å resolution. The YAP 14-3-3-binding motif is revealed for the first time using crystallographic tools.
Tom70 family members may exhibit structural plasticity when complexed with Hsp70/Hsp90. This structural plasticity enables Tom70 to accommodate various precursor substrates for mitochondrial translocation.
The type III secretion system needle-tip protein BipD has been crystallized in a form that diffracts X-rays to 1.5 Å resolution and the structure has been refined to an R factor of 16.1% and an R free of 19.8% at this resolution. The putative antiparallel dimer interface that was observed in earlier structures is conserved.
A new crystal form of Lys48-linked diubiquitin was obtained and its structure was determined by X-ray crystallography to 1.6 Å resolution.
An inhibited conformation of the protein kinase domain (KD) of Snf1 is observed. The auto-inhibitory domain (AID) is disordered.
When compared with their E. coli homologue, two X-ray crystal structures of T. maritima endonuclease IV differing in the composition of the trinuclear metal site point to the importance of the trinuclear site and its modulation among species to the function of this enzyme in the AP endonuclease IV family.
Structures of binary and ternary Dpo4 DNA polymerase complexes crystallized in the presence of Mg2+ have been determined. Comparisons with the corresponding Ca2+-form structures revealed subtle changes in the active-site geometry.
The molecular structure of a complex of an anthraquinone derivative and the oligonucleotide d(UBrAGG) is presented. The anthraquinone molecules are stacked. Isolated base pairs are intercalated in the stack of drug molecules.
The structure of an α-spectrin SH3-domain mutant with a stabilized hydrophobic core and distal loop has been solved at 1 Å resolution.
The crystal structure of the tetragonal form of the non-self-complementary DNA sequence d[GCG(xT)GCG]/d(CGCACGC) with one incorporated CeNA (xT) moiety has been solved and is compared with the high-resolution orthorhombic form.
The structure of Ca2+-bound EF-hand protein S100A2 was determined by calcium and sulfur SAD at a wavelength of 0.90 Å.
A galactose-specific lectin purified from the seeds of bitter gourd (M. charantia) has been crystallized and preliminary X-ray study of the crystals has been carried out.
The catalytic domain of CHBI was purified from a cellular extract of T. harzianum. Diffraction-quality crystals were obtained and a native X-ray data set was collected using a synchrotron source.
The expression, purification, crystallization and preliminary crystallographic analysis of the PaaAC complex is reported. This is the main component of the E. coliphenylacetyl-coenzyme A oxygenase complex.
A common biotransformation of arsenic is methylation to monomethylated, dimethylated and trimethylated species, which is catalyzed by the ArsM (or AS3MT) arsenic(III) S-adenosylmethionine methyltransferase. ArsM from the acidothermophilic alga Cyanidioschyzon sp. 5508 was expressed, purified and crystallized by the hanging-drop vapor-diffusion method and diffraction data were collected to 1.76 Å...
Crystals of 5-aminolaevulinic acid dehydratase from B. subtilis are tetragonal, belonging to space group P42212, and diffract to 2.7 Å resolution.
The N-terminal PAS domains from the eukaryotic EAG potassium channels are thought to have a regulatory function. Here the expression, purification, crystallization and preliminary crystallographic characterization of two of these domains are described.
The E. coli antitoxin MqsA (YgiT/b3021) has been cocrystallized with mqsRA promoter DNA. A native data set has been collected to a resolution of 2.1 Å.
Formate oxidase from A. oryzae RIB40 was crystallized and diffraction data were collected to a resolution of 2.4 Å.
In this study, the human condensin SMC2 hinge domain with short coiled coils was cloned, expressed, purified and crystallized in the orthorhombic space group C222 in native and SeMet-derivatized forms.
In this study, the core region of Ara h 1, one of the major peanut allergens, has been overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.25 Å resolution.
Crystallization of AcnR, a repressor of the aconitase gene in Corynebacterium glutamicum, is reported. Intentional manual scratching of the crystallization plates was applied to induce heterogeneous nucleation.
The catalytic domain of a hyperthermostable endo-1,4-β-d-mannanase from T. petrophila RKU-1 has been cloned, overexpressed in E. coli cells, purified and crystallized in two distinct crystalline forms by the sitting-drop vapour-diffusion method.
The carbonic anhydrase αCA1 from C. reinhardtii is a dimeric class αCA enzyme with post-translational glycosylation at three asparagine residues and proteolytic removal of a short peptide. The mature enzyme has been crystallized, MAD data have been collected to 1.88 Å resolution and a preliminary solution of the crystal structure has been obtained.
In this study, the glucansucrase from the dental caries pathogen S. mutans was purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant.
Cu,Zn superoxide dismutase from the thermophilic fungus C. thermophilum was expressed in P. pastoris, purified and crystallized. A complete data set was collected to 1.9 Å resolution using synchrotron radiation.
The C-terminal domain of M. tuberculosis LexA has been crystallized and its structure has been solved.
The expression, purification, crystallization and preliminary X-ray diffraction analysis of pili-specific and housekeeping sortases from S. agalactiae are reported.
The crystallization and primary crystallographic analysis of B. megaterium tyrosinase is reported. The purified protein was crystallized in the absence or presence of zinc ions to a resolution of 2.0 Å.
IMP dehydrogenase from C. neoformans and C. gattii has been crystallized in complex with the substrate IMP and the cofactor NAD+.
OleC crystals belonged to space group P3121 or P3221 and diffracted to 3.4 Å resolution at a third-generation synchrotron X-ray source.
The preliminary crystallographic analysis of the N-terminal domain of FILIA is described in this paper. FILIA is a component of subcortical maternal complex, which plays critical roles in embryogenesis.
GenX, a lysyl-tRNA synthetase paralogue from Escherichia coli, has been overexpressed in E. coli, purified by three chromatographic steps and cocrystallized with a lysyl adenylate analogue (LysAMS) by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant.
Native FrpD43–271 and selenomethionine-derivative FrpD43–271 proteins were purified, crystallized and diffracted to resolutions of 2.25 and 2.00 Å, respectively.
The crystallization of the homologous recombination mediators Swi5 and Sfr1 from fission yeast is reported.
Autotaxin (ATX), a pyrophosphatase/phosphodiesterase enzyme, is a promising drug target for many indications and is only distantly related to enzymes of previously determined structure. Here, the cloning, expression, purification, crystallization and preliminary diffraction analysis of ATX are reported.
Autotaxin, a four-domain ~100 kDa mammalian glycoprotein, was expressed in stably transfected mammalian cells, purified from the medium and crystallized. Diffraction data from micrometre-thick crystal plates were collected on various European synchrotron beamlines and are presented and analysed.