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Preliminary X-ray Diffraction Study (preliminary + x-ray_diffraction_study)
Selected AbstractsCrystallization and preliminary X-ray diffraction study of mammalian mitochondrial seryl-tRNA synthetaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2004Sarin Chimnaronk The mitochondrial seryl-tRNA synthetase (mt SerRS) from Bos taurus was overexpressed in Escherichia coli and crystallized using the sitting-drop vapour-diffusion method. Crystals grew in a very narrow range of conditions using PEG 8000 as precipitant at room temperature. An appropriate concentration of lithium sulfate was critical for crystal nucleation. Crystals diffracted well beyond a resolution of 1.6,Å and were found to belong to the orthorhombic space group C2221, with unit-cell parameters a = 79.89, b = 230.42, c = 135.60,Å. There is one dimer (Mr, 113,kDa) in the asymmetric unit, with a solvent content of 55%. Efforts to solve the phase problem by molecular replacement are under way. [source] Purification, crystallization and preliminary X-ray diffraction study of human ribosomal protein L10 core domainACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 11 2007Mitsuhiro Nishimura Eukaryotic ribosomal protein L10 is an essential component of the large ribosomal subunit, which organizes the architecture of the aminoacyl-tRNA binding site. The human L10 protein is also called the QM protein and consists of 214 amino-acid residues. For crystallization, the L10 core domain (L10CD, Phe34,Glu182) was recombinantly expressed in Escherichia coli and purified to homogeneity. A hexagonal crystal of L10CD was obtained by the sitting-drop vapour-diffusion method. The L10CD crystal diffracted to 2.5,Å resolution and belongs to space group P3121 or P3221. [source] Purification, crystallization and preliminary X-ray diffraction study on pyrimidine nucleoside phosphorylase TTHA1771 from Thermus thermophilus HB8ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2007Katsumi Shimizu Pyrimidine nucleoside phosphorylase (PYNP) catalyzes the reversible phosphorolysis of pyrimidines in the nucleotide-synthesis salvage pathway. In order to study the structure,thermostability relationship of this enzyme, PYNP from the extreme thermophile Thermus thermophilus HB8 (TTHA1771) has been cloned, overexpressed and purified. The TTHA1771 protein was crystallized at 291,K using the oil-microbatch method with PEG 4000 as a precipitant. A native data set was collected to 1.8,Å resolution using synchrotron radiation. The crystal belongs to the monoclinic space group P21, with unit-cell parameters a = 58.83, b = 76.23, c = 103.86,Å, , = 91.3°. [source] Crystallization and preliminary X-ray diffraction study of a cell-wall invertase from Arabidopsis thalianaACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2005Maureen Verhaest Cell-wall invertase 1 (AtcwINV1), a plant protein from Arabidopsis thaliana which is involved in the breakdown of sucrose, has been crystallized in two different crystal forms. Crystal form I grows in space group P31 or P32, whereas crystal form II grows in space group C2221. Data sets were collected for crystal forms I and II to resolution limits of 2.40 and 2.15,Å, respectively. [source] Crystallization and preliminary X-ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesisACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2005Jiro Harada The S -adenosylmethionine-dependent methyltransferase BchU is an enzyme involved in the bacteriochlorophyll c biosynthetic pathway and catalyzes methylation at the C-20 position of the chlorin moiety. Recombinant Chlorobium tepidum BchU overproduced in Escherichia coli was purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belonged to the hexagonal space group P6122 or P6522, with unit-cell parameters a = b = 81.5, c = 250.7,Å. A native data set was collected to 2.27,Å resolution using synchrotron radiation at SPring-8. [source] Crystallization and preliminary X-ray diffraction study of thermostable RNase HIII from Bacillus stearothermophilusACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2005Hyongi Chon A thermostable ribonuclease HIII from Bacillus stearothermophilus (Bst RNase HIII) was crystallized and preliminary crystallographic studies were performed. Plate-like overlapping polycrystals were grown by the sitting-drop vapour-diffusion method at 283,K. Native X-ray diffraction data were collected to 2.8,Å resolution using synchrotron radiation from station BL44XU at SPring-8. The crystals belong to the orthorhombic space group P21212, with unit-cell parameters a = 66.73, b = 108.62, c = 48.29,Å. Assuming one molecule per asymmetric unit, the VM value was 2.59,Å3,Da,1 and the solvent content was 52.2%. [source] | ||||||||||