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The crystal structures of engineered C. botulinum neurotoxin–SNARE derivatives have been and exhibit strong stability of the LHn fragment.
Recombinant hyperthermophilic β-glucosidase from P. furiosus was crystallized. The crystal structure was solved to a resolution of 2.35 Å.
The crystal structure of At2g44920, a pentapeptide repeat protein (PRP) from Arabidopsis thaliana, has been determined at 1.7 Å resolution. The structure represents the first PRP protein whose subcellular localization has been experimentally confirmed to be the thylakoid lumen of a plant species.
The crystallographic structures of the subunit B mutants F427W and F508W of the Pyrococcus horikoshii OT3 of the A1AO ATP synthase reveal that the exact volume of the adenine ribose binding pocket is essential for ATP-/ADP-binding.
A new 1.8 Å resolution structure of α1-antitrypsin demonstrates structural variability within an allosteric site in the molecule.
Structural analysis of the catalytic module of Caldicellulosiruptor bescii family 3 pectate lyase shows that this new structure is very similar to the previously solved structure of a family 3 pectate lyase from Bacillus sp. strain KSM-P15.
The structure of LsrB from Y. pestis complexed with autoinducer-2 (AI-2) has been determined at 1.75 Å resolution. Bound AI-2 adopts the (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran conformation, which is the same conformation as is observed in the S. typhimurium and S. meliloti LsrB–AI-2 structures.
The crystal structure of the DNA sequence d(CGGGTACCCG)4 as a four-way Holliday junction and its interaction with a calcium ion are described.
The structure of NFeoB from S. thermophilus harbouring an N11A mutation has been determined to 1.85 Å resolution.
The purification, crystallization and X-ray structure analysis of human L30e are presented here.
The crystal structure of the H107R variant of the extracellular domain of mouse NKR-P1A was determined using X-ray diffraction from a merohedrally twinned crystal.
SpFcsU is a fucose mutarotase from S. pneumoniae that links the harvesting of fucose from glycans by glycoside hydrolases to processing of the fucose monosaccharide by subsequent enzymes in a fucose-utilization pathway. Here, the decameric structure of SpFcsU in complex with fucose is described.
The crystallization of the OmpA periplasmic domain from A. baumannii is described.
A novel haemagglutinin from Jatropha curcas seeds is purified and crystallized. X-ray diffraction data collected from the rod-shaped crystals were processed in the orthorhombic space group P212121 and the crystals diffracted to 2.8 Å resolution at 103 K.
Dihydrodipicolinate synthase from the common grapevine V. vinifera has been cloned, expressed, purified and crystallized in the presence of the substrate pyruvate by in-drop hexahistidine-tag cleavage. A diffraction data set has been collected to a resolution of 2.2 Å.
S. mutans dextranase was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 1.6 Å and belonged to space group P21.
The crystallization and preliminary X-ray diffraction analysis of crinumin, a plant serine protease, is reported.
β-Ketoacyl-acyl carrier protein synthase I (XoFabB) from X. oryzae pv. oryzae (Xoo) plays a crucial role in fatty-acid synthesis and has been considered as a target for the development of antibacterial agents against Xoo. XoFabB was expressed, purified and crystallized to determine its atomic resolution structure.
A hyperthermophilic adenylosuccinate synthetase from P. horikoshii OT3, which is 90–120 amino acids shorter than those from the vast majority of organisms, was expressed, purified and crystallized and X-ray diffraction data were collected to 2.5 Å resolution.
Shikimate dehydrogenase from A. fulgidus has been overexpressed and crystallized. X-ray diffraction data have been collected to 2.8 Å resolution.
In this study, a putative glucokinase/hexokinase from T. thermophilus was purified and crystallized. Diffraction data were collected and processed to 2.02 Å resolution.
This article reports the molecular cloning, protein expression and purification, crystallization and preliminary X-ray crystallographic analysis of the vibriobactin synthetase VibE from V. cholerae.
Peptidyl-tRNA hydrolase from E. coli has been crystallized in complex with the acceptor-TΨC domain of tRNA. Diffraction data have been collected and processed to 2.4 Å resolution.
Penicillin G acylase from the Gram-positive bacterium B. megaterium was crystallized and X-ray diffraction from these crystals could be substantially improved by slight dehydration through a long cryo-soak.
A C2 protein from A. thaliana has been crystallized by the hanging-drop vapour-diffusion method and a native data set has been collected at 2.4 Å resolution.
The Saccharomyces cerevisiae NAD+-dependent deacetylase HST1156–503 was expressed and crystallized. Crystals grown by the hanging-drop vapour-diffusion method diffracted to 2.90 Å resolution.
Expression, purification and crystallization of Srr-1-K4BD, a human keratin 4-binding domain of serine-rich repeat protein 1 from S. agalactiae, was carried out. Native crystals of Srr-1-K4BD diffracted to 3.8 Å resolution using synchrotron radiation.
Crustacean hyperglycaemic hormone from the kuruma prawn M. japonicus was crystallized by the sitting-drop vapour-diffusion method in its weakly active precursor form which has an extra glycine residue at the C-terminus. The crystals belonged to the orthorhombic space group P212121 and diffracted to 1.95 Å resolution.
Tthe cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of a bifunctional purine-biosynthesis enzyme from E. coli which possesses aminoimidazole-4-carboxamide ribonucleotide transformylase and IMP cyclohydrolase activities are reported.
A thermostable multicopper oxidase from Thermus thermophilus HB27 (Tth-MCO) has been successfully crystallized using the sitting-drop and hanging-drop vapour-diffusion methods.
The crystallization of Chlorella dUTPase is described. The crystallization of plant dUTPase isozymes and their parameterization is discussed.
This report describes the crystallization and X-ray diffraction analysis of two different allelic variants of the AvrM effector from flax rust.
The crystallization and preliminary X-ray diffraction analysis of Val57 mutants of human cystatin C, designed to assess the influence of changes in the properties of loop L1 on dimerization propensity, are reported.
The major group 7 allergen, Der f 7, from the dust mite Dermatophagoides farinae has been crystallized and diffracted X-rays to a resolution of 2.24 Å.
The cysteine free derivative of the arsenic repressor ArsR from Corynebacterium glutamicum was expressed, purified, crystallized and X-ray diffraction data up to 1.86 Å resolution have been collected. The crystals belonged to the space group P4 with the unit-cell parameters a = b = 41.84, c = 99.47 Å.
Two types of His6-tag-fused HP0902 protein from H. pylori 26695 have been crystallized and X-ray diffraction data were obtained at 1.4 and 2.5 Å resolution.
B. pseudomallei BPSL1549 has been overexpressed in E. coli, purified and crystallized.
Fluorescence recovery protein from Synechocystis PCC 6803 plays a key role in the orange carotenoid protein-related photoprotective mechanism in cyanobacteria. The full-length form and a truncated form were overexpressed, purified and crystallized, and diffraction was observed to 2.75 Å resolution.
Aldo-keto reductase 1B3 (AKR1B3) produced in Escherichia coli has been crystallized in complex with NADPH by the sitting-drop vapour-diffusion method.
Crystals of native and selenomethionine-substituted C-reactive protein from zebrafish diffracted to 2.3 and 1.7 Å resolution, respectively, and belonged to space group R3 with one molecule per asymmetric unit. The Matthews coefficient was calculated to be 3.28 Å3 Da−1.
The acyl-CoA carboxylase β subunit (ACCD6) of M. tuberculosis has been crystallized and preliminary X-ray crystallographic analysis has been performed.
Diffraction-quality crystals of the peroxidase from the palm tree C. excelsa were obtained and a native X-ray diffraction data set was collected at a synchrotron source.
The chemotaxis response regulator CheY4 from V. cholerae has been cloned, overexpressed, purified and crystallized in monoclinic and hexagonal space groups; the crystals diffracted to 1.67 and 1.9 Å resolution, respectively.
Crystals of the helicase domain from a tomato mosaic virus replication protein obtained using the hanging-drop vapour-diffusion method at 285 K diffracted X-rays to 2.05 Å resolution. They belonged to the orthorhombic space group P212121, with unit-cell parameters a = 85.8, b = 128.3, c = 40.7 Å.
A 79 kDa fragment of FlgE from C. jejuni has been crystallized.
Acetate kinase from S. typhimurium was crystallized in two crystal forms that diffracted to 2.70 Å (form I) and 1.90 Å (form II) resolution.
Cerium was used to enhance the anomalous signal in hen egg-white lysozyme crystals and led to successful in-house SAD phasing.
Dodecyl-β-d-selenomaltoside in a leukotriene C4 synthase crystal exhibited sufficient anomalous diffraction for multiwavelength anomalous diffraction phasing.
A correction to the article by Ortíz et al. [(2011), Acta Cryst. F67, 1457–1461].