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M Sodium Acetate (m + sodium_acetate)
Selected AbstractsCrystallization and preliminary X-ray characterization of a thermostable pectate lyase from Thermotoga maritimaACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2002Michael A. McDonough Pectate lyase is an enzyme involved in the degradation of the pectate portion of the primary plant cell wall. A recombinant pectate lyase from Thermotoga maritima where three of the four cysteine residues have been mutated (C132I, C156N, C194L) has been crystallized. Crystals of the same morphology and trigonal space group R3 with similar unit-cell parameters were obtained under two different conditions. The first, 0.3,M (NH4)H2PO4 pH 4.2, gave crystals with a maximum size of 0.4 × 0.2 × 0.2,mm in one week that diffracted to a resolution of 1.87,Å and had unit-cell parameters a = b = 80.6, c = 148.8,Å. The second, 0.1,M sodium acetate, 6%(w/v) PEG 4000 pH 6.5, gave the same size crystals in two weeks that diffracted to a resolution of 2.1,Å and had unit-cell parameters a = b = 80.0, c = 150.1,Å. [source] Crystallization and preliminary X-ray diffraction studies of hyperthermophilic archaeal Rieske-type ferredoxin (ARF) from Sulfolobus solfataricus P1ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2010Asako Kounosu The hyperthermophilic archaeal Rieske-type [2Fe,2S] ferredoxin (ARF) from Sulfolobus solfataricus P1 contains a low-potential Rieske-type [2Fe,2S] cluster that has served as a tractable model for ligand-substitution studies on this protein family. Recombinant ARF harbouring a pET30a vector-derived N-terminal extension region plus a hexahistidine tag has been heterologously overproduced in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using 0.05,M sodium acetate, 0.05,M HEPES, 2,M ammonium sulfate pH 5.5. The crystals diffracted to 1.85,Å resolution and belonged to the tetragonal space group P43212, with unit-cell parameters a = 60.72, c = 83.31,Å. The asymmetric unit contains one protein molecule. [source] Overexpression, purification, crystallization and preliminary structural studies of p -coumaric acid decarboxylase from Lactobacillus plantarumACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2007Blanca De Las Rivas The substrate-inducible p -coumaric acid decarboxylase (PDC) from Lactobacillus plantarum has been overexpressed in Escherichia coli, purified and confirmed to possess decarboxylase activity. The recombinant His6 -tagged enzyme was crystallized using the hanging-drop vapour-diffusion method from a solution containing 20%(w/v) PEG 4000, 12%(w/v) 2-propanol, 0.2,M sodium acetate, 0.1,M Tris,HCl pH 8.0 with 0.1,M barium chloride as an additive. Diffraction data were collected in-house to 2.04,Å resolution. Crystals belonged to the tetragonal space group P43, with unit-cell parameters a = b = 43.15, c = 231.86,Å. The estimated Matthews coefficient was 2.36,Å3,Da,1, corresponding to 48% solvent content, which is consistent with the presence of two protein molecules in the asymmetric unit. The structure of PDC has been determined by the molecular-replacement method. Currently, the structure of PDC complexed with substrate analogues is in progress, with the aim of elucidating the structural basis of the catalytic mechanism. [source] Expression, purification and crystallization of a novel nonstructural protein VP9 from white spot syndrome virusACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2006Yang Liu The nonstructural protein VP9 from white spot syndrome virus (WSSV) has been identified and expressed in Escherichia coli. To facilitate purification, a cleavable His6 tag was introduced at the N-terminus. The native protein was purified and crystallized by vapour diffusion against mother liquor containing 2,M sodium acetate, 100,mM MES pH 6.3, 25,mM cadmium sulfate and 3% glycerol. Crystals were obtained within 7,d and diffracted to 2.2,Å; they belonged to space group P212121, with unit-cell parameters a = 74.13, b = 78.21, c = 78.98,Å and four molecules in the asymmetric unit. The selenomethionine-labelled protein produced isomorphous crystals that diffracted to approximately 3.3,Å. [source] | ||||||||||