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A general tetramerization and oligomerization scheme is proposed for BenM and other LysR-type transcriptional regulators based on two newly characterized structures of the effector-binding domain of BenM. An analysis of these structures in the light of other LysR-type structures may explain the general solubility problems associated with this protein family.
Using single-wavelength anomalous dispersion data obtained from a gold-derivatized crystal, the X-ray crystal structure of the protein 067745_AQUAE from the prokaryotic organism Aquifex aeolicus has been determined to a resolution of 2.0 Å.
Human nicotinamide phosphoribosyltransferase has been crystallized using microseeding methods and X-ray diffraction data have been collected at 2.0 Å resolution.
Preliminary crystallographic data for 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from P. putida 33/1 are reported.
Preliminary crystallographic data are reported for 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from A. nitroguajacolicus Rü61a.
Crystals of an MHC class I molecule bound to naturally occurring peptide variants from the dengue virus NS3 protein contained high levels of solvent and required optimization of cryoprotectant and dehydration protocols for each complex to yield well ordered diffraction, a process facilitated by the use of a free-mounting system.
l-2-Keto-3-deoxyarabonate dehydratase was overexpressed, purified and crystallized at 291 K using the hanging-drop vapour-diffusion method.
The 24 kDa egg lectin of Chinook salmon (Oncorhynchus tshawytscha) was purified by affinity chromatography from salmon eggs and crystallized by the hanging-drop vapor-diffusion method using 15/4 EO/OH (pentaerythritol ethoxylate) as a precipitant.
Attempts to crystallize succinyl-CoA synthetase from the thermophile T. aquaticus were thwarted by proteolysis of the β-subunit and preferential crystallization of a truncated form. Crystals of the full-length enzyme were grown after the purification protocol was modified to include frequent additions of protease inhibitors.
Crystals of the rat histone H10 globular domain have been grown in the trigonal space group P3121 and diffracted to a resolution of 1.98 Å. Molecular-replacement solutions were identified and refinement has been started.
A RecB-like nuclease from the archaeon Pyrococcus abyssi was expressed, purified and crystallized. The crystals belong to the orthorhombic space group C2221 with a = 81.5, b = 159.8, c = 100.8 Å, and a native data set was collected to 2.65 Å resolution.
The first crystallization of deoxyuridine triphosphate nucleotidohydrolase from plant, Arabidopsis thaliana, has been performed. An additive, taurine, was effective in producing the single crystal.
A putative UDP-N-acetyl-d-mannosamine dehydrogenase from P. horikoshii OT3 has been crystallized in space group P21, with unit-cell parameters a = 80.28, b = 69.24, c = 83.10 Å, β = 114.4°. X-ray diffraction data have been collected to 1.80 Å resolution.
The cloning, expression, purification and crystallization of wild-type AlgK from P. fluorescens is described. The crystals diffract to 2.5 Å resolution.
The mRNA-binding domain of E. coli selenocysteine-specific elongation factor SelB (residues 478–614; SelB-WH3/4) was overproduced in E. coli and its cognate mRNA ligand, 23 nucleotides of the SECIS RNA hairpin, was prepared by in vitro transcription. The purified SelB-WH3/4–SECIS RNA complex crystallized in space group C2 and diffracted to 2.3 Å.
Palustrisredoxin reductase (RPA3782, PuR), a flavin-dependent ferredoxin reductase, is an essential component of the Class I cytochrome P450 systems in Rhodopseudomonas palustris CGA009. Crystals of PuR that diffract to 2.2 Å resolution have been obtained.
The avian reovirus double-stranded RNA-binding and core protein σA has been crystallized in space group P1, with unit-cell parameters a = 103.2, b = 129.9, c = 144.0 Å, α = 93.8, β = 105.1, γ = 98.2°. A complete data set has been collected to 2.3 Å resolution and analyzed.
Crystals of the enzyme hexokinase 1 from the yeast K. lactis (KlHxk1) suitable for X-ray analysis were obtained in various space groups.
Full-length Mos1 transposase has been crystallized in a complex with inverted-repeat DNA. Crystals diffract to 3.25 Å resolution and display noncrystallographic twofold symmetry.
A bacterial UMP kinase from the plant pathogen X. campestris pathovar campestris has been overexpressed in E. coli, purified and crystallized in a strong magnetic field. The crystals diffracted to 2.35 Å.
S. cerevisiae Atg10, an E2-like enzyme that mediates the conjugation reaction between Atg12 and Atg5, was crystallized and diffracted to 2.3 Å resolution.
The glucose dehydrogenase (GDH) protein from T. thermophilus HB8 was cloned, expressed, purified and crystallized. GDH crystals belong to space group P21 and diffract to 1.9 Å resolution.
Preliminary crystallographic data are reported for the third SRP GTPase FlhF from Bacillus subtilis.
As part of work on S. aureus, the crystallization of Sar2028, a protein that is upregulated in MRSA, is reported.