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The structure of E. coli dihydrodipicolinate synthase cocrystallized with oxaloacetic acid has been solved at a resolution of 2.0 Å. The structure was found to contain a pyruvate molecule bound at the active site rather than oxaloacetate.
The crystal structure of the signal receiver domain of NarL from M. tuberculosis, a putative nitrate response regulator involved in the regulation of anaerobic metabolism, has been determined to 1.9 Å resolution.
The crystal structure of the wild-type BCL6 POZ domain confirms the structure of previously reported mutant proteins and will have relevance for the design of therapeutics that target BCL6 POZ-domain function.
The structure of a xenon derivative of E. coli copper amine oxidase confirms the pathway of oxygen entry to the buried active site proposed for this class of enzymes.
Two manganese superoxide dismutase enzymes isolated from the eukaryote C. elegans have been characterized and their structures determined. The closely related structures reveal a striking similarity to manganese superoxide dismutase found in humans.
Xoo0352, which encodes d-alanine-d-alanine ligase A (DdlA), from X. oryzae pv. oryzae was cloned, purified and crystallized. Preliminary X-ray crystallographic analysis of DdlA crystals was performed.
Crystals of phospholipase A1 from hornet (V. basalis) venom were obtained that diffracted X-rays to a resolution of at least 2.5 Å resolution.
Glucosyl-3-phosphoglycerate synthase (GpgS) is a key enzyme that catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in Mycobacterium spp. Here, the crystallization and preliminary crystallographic analysis of GpgS from M. tuberculosis and of its complex with UDP are reported.
The plasma-membrane Na+/Ca2+ exchanger (NCX) regulates intracellular Ca2+ levels in cardiac myocytes. Two Ca2+-binding domains (CBD1 and CBD2) exist in the large cytosolic loop of NCX. Recombinant CBD1 (NCX1 372–508) with a molecular weight of 16 kDa has been crystallized by the sitting-drop vapour-diffusion method at 293 K.
Bacterial blight is a destructive disease of rice that is caused by X. oryzae pv. oryzae (Xoo). Dehydroquinate synthase, which is the second enzyme of the shikimate pathway, was cloned from Xoo1243 (aroB), purified and crystallized in order to elucidate its three-dimensional structure.
Monoclinic crystals of the ρ-class glutathione S-transferase from L. elliptica were obtained in both glutathione- and CDNB-complexed forms.
The cloning, expression, purification, crystallization and preliminary X-ray characterization of an l-N-carbamoylase from G. stearothermophilus are described.
Isocitrate dehydrogenase 2 from M. tuberculosis was cloned, expressed, purified and crystallized. A complete data set has been collected to 3.25 Å resolution.
Bacterial blight is the most destructive bacterial disease of rice and is caused by X. oryzae pv. oryzae (Xoo). Xoo0880 (FabD), a malonyl-CoA–acyl carrier protein transacylase, from Xoo was cloned, purified and crystallized.
A thermophilic bacterial homologue of mitoNEET (a mammalian mitochondrial outer membrane protein) from T. thermophilus HB8 (open reading frame TTHA0026; Tth-NEET0026) has been identified as a water-soluble prototypal [2Fe–2S] protein and crystallized. The bipyramidal crystals of the recombinant Tth-NEET0026 diffracted to 1.80 Å resolution using synchrotron radiation.
The NodS N-methyltransferase, an enzyme participating in the biosynthesis of the bacterial nodulation (Nod) factor necessary to establish symbiotic nitrogen fixation with a legume plant host, has been crystallized in the apo form as well as in complex with SAH. SAH is a byproduct of SAM degradation during the SAM-dependent methylation reaction.
A 1.35 Å resolution data set was collected from a crystal of the periplasmic GABA receptor Atu2422 from A. tumefaciens. Atu2422 adopts a closed Venus flytrap conformation.
Crystals of human breast cancer metastasis Suppressor 1 N-terminal coiled-coil have been obtained and diffracted to 2.0 Å.
The human androgen receptor ligand-binding domain has been crystallized as a ternary complex with a coactivator-like undecapeptide and two different synthetic ligands.
The transfer of sugars is an important process in both biology and biotechnology; the first crystallization of a rhamnosyltransferase is reported.
In this study, the TrmE protein from the pathogenic bacterium S. aureus was overexpressed and crystallized (space group I23, unit-cell parameters a = b = c = 229.47 Å, α = β = γ = 90°). Diffraction data were collected to 2.9 Å resolution using synchrotron radiation.
Hyperthermostable P. horikoshii endoglucanase was produced as a truncated form that maintained enzymatic properties; it was crystallized and its crystals diffracted to 1.78 Å resolution.
Mhp1, a hydantoin transporter from M. liquefaciens, was purified and crystallized. Diffraction data were collected to 2.85 Å resolution; the crystal belonged to the orthorhombic space group P212121.
The second RanBP2-type zinc finger from ZRANB2 has been crystallized in complex with a single-stranded RNA target sequence.
The first crystallographic study of a member of the NLP (Nep1-like protein) toxin and elicitor protein family is reported.
Phosphoglucose isomerase from B. subtilis has been purified and crystallized. The diffraction quality of the crystal was improved by using a flash-annealing technique and 1.9 Å resolution in-house X-ray data were collected.
Crystals of the Sox17 HMG domain bound to LAMA1 enhancer DNA-element crystals that diffracted to 2.75 Å resolution were obtained.