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Cloning, expression, crystallization and preliminary X-ray analysis of the DNA-binding protein Sso10a from Sulfolobus solfataricus

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 2003年第7期59卷 1320-1322页

作者： Teale, MJ Kahsai, M Singh, SK Edmondson, SP Gupta, R Shriver, JW Meehan, E Univ Alabama Dept Chem Struct Biol Lab Huntsville AL 35899 USA So Illinois Univ Sch Med Dept Biochem & Mol Biol Carbondale IL 62901 USA

The gene for the DNA-binding protein Sso10a from the hyperthermophilic archaeon Sulfolobus solfataricus was cloned and overexpressed in Escherichia coli. Crystals of the purified protein have been grown that diffract to beyond 2.15 Angstrom resolution. The protein crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 57.24, b = 60.16, c = 69.96 Angstrom. With one dimer per asymmetric unit, the crystal to volume per protein mass (V-M) is 2.9 Angstrom(3) Da(-1) and the solvent content is similar to57%. Complete X-ray diffraction native data were collected from a single crystal and processed to 2.15 Angstrom.

关键词：氨基酸序列古细菌蛋白质类/化学古细菌蛋白质类/遗传学古细菌蛋白质类/分离和提纯克隆分子结晶 DNA结合蛋白质类/化学 DNA结合蛋白质类/遗传学 DNA结合蛋白质类/分离和提纯序列比对硫化叶菌属/化学 X线衍射

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Electrophoresis of proteins and protein-protein complexes in a native agarose gel

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ANALYTICAL BIOCHEMISTRY 2000年第1期282卷 147-149页

作者： Kim, R Yokota, H Kim, SH Univ Calif Berkeley Lawrence Berkeley Lab Div Phys Biocsci Berkeley CA 94720 USA Univ Calif Berkeley Dept Chem Berkeley CA 94720 USA

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Expression, purification, crystallization and preliminary X-ray diffraction studies of bacterial and archaeal L4 ribosomal proteins

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 2000年第5期56卷 645-647页

作者： Worbs, M Wahl, MC Max Planck Inst Biochem Abt Strukturforsch D-82152 Martinsried Germany

Ribosomal protein L4 is implicated in the peptidyltransferase activity of the ribosome and in certain bacteria it regulates the transcription and translation of the 11-gene S10 operon. The genes for the L4 ribosomal proteins from the hyperthermophilic bacterium Thermotoga maritima and the halophilic archaeon Haloarcula marismortui have been PCR amplified from genomic DNA and cloned under the control of a T7 promoter to generate overexpressing Escherichia coli strains. For both proteins, efficient purification procedures were developed to yield material suitable for crystallization trials. Crystals of T. maritima L4 were obtained in the orthorhombic space group P2(1)2(1)2(1), with one molecule per asymmetric unit, diffracting to 1.7 Angstrom resolution with synchrotron radiation. Crystals of H. marismortui L4 belonged to the trigonal space group P3(1)21 or P3(2)21 and diffracted to 3.2 Angstrom resolution with a rotating-anode source, presumably containing three molecules per asymmetric unit. The results demonstrate that for certain halophilic proteins the same purification and crystallization procedures can be employed as for conventional proteins.

关键词：古细菌蛋白质类/化学古细菌蛋白质类/遗传学古细菌蛋白质类/分离和提纯细菌蛋白质类/化学细菌蛋白质类/遗传学细菌蛋白质类/分离和提纯克隆分子结晶结晶学 X线/方法死海嗜盐古细菌/遗传学蛋白质构象重组蛋白质类/化学重组蛋白质类/分离和提纯核糖体蛋白质类/化学核糖体蛋白质类/遗传学核糖体蛋白质类/分离和提纯喜温海洋杆菌/遗传学

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Crystallization and preliminary X-ray study of Pk-REC from a hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 2000年第5期56卷 648-649页

作者： Harata, K Ishii, N Rashid, N Masaaki, M Imanaka, T Natl Inst Biosci & Human Technol Biomol Dept Tsukuba Ibaraki 3058566 Japan Kyoto Univ Grad Sch Engn Dept Synthet Chem & Biol Chem Sakyo Ku Kyoto 6068501 Japan Osaka Univ Grad Sch Engn Dept Mat & Life Sci Suita Osaka 5650871 Japan

Pk-REC is a protein which binds to DNA and catalyzes the central step of recombination and repair. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG as a precipitant. Two orthorhombic crystal forms I and II with the same space group P2(1)2(1)2(1) were obtained at pH 8.0 using PEG 3000 and PEG 550 monomethylether, respectively. The unit-cell parameters were a = 151, b = 174, c = 241 Angstrom for form I and a = 151, b = 176, c = 300 Angstrom for form II, indicating that the asymmetric unit contains more than 20 molecules.

关键词：古细菌蛋白质类/化学古细菌蛋白质类/遗传学古细菌蛋白质类/分离和提纯克隆分子结晶结晶学 X线/方法大肠杆菌热温度氢离子浓度聚乙烯二醇类焦球菌属/遗传学重组蛋白质类/化学重组蛋白质类/分离和提纯

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Crystallization and preliminary X-ray diffraction analysis of a cytochrome P450 (CYP119) from Sulfolobus solfataricus

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ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 2000年第9期56卷 1173-1175页

作者： Park, SY Yamane, K Adachi, S Shiro, Y Weiss, KE Sligar, SG RIKEN Harima Inst Sayo Hyogo 6795148 Japan Univ Illinois Beckman Inst Adv Sci & Technol Urbana IL 61801 USA

CYP119 is a cytochrome P450 with a molecular weight of 43 kDa which has been isolated from the thermophilic archaeon Sulfolobus solfataricus. This enzyme is extremely stable to high temperature and high pressure. The first crystallization and preliminary crystallographic study of CYP119 is reported here. Crystals of CYP119 were obtained by the sitting-drop vapour-diffusion method using a precipitant solution containing 20%(w/v) PEG 4000 and 0.2 M sodium thiocyanate at pH 6.4. Using synchrotron radiation, the CYP119 crystal diffracted to 1.84 Angstrom resolution. It belongs to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 86.17 (0.07), c = 221.11 (0.04) Angstrom, in which the numbers in parentheses describe the standard deviations. Assuming two molecules of the CYP119 per asymmetric unit, the calculated molar volume (V-m) is 2.38 Angstrom(3) Da(-1). Bijvoet and dispersive anomalous difference Patterson maps show a clear peak corresponding to the haem irons. The complete crystallographically defined structure is currently in progress using MIR (multiple isomorphous replacement) and MAD (multiwavelength anomalous diffraction) techniques.

关键词：古细菌蛋白质类/化学古细菌蛋白质类/遗传学古细菌蛋白质类/分离和提纯结晶结晶学 X线细胞色素P450酶系统/化学细胞色素P450酶系统/遗传学细胞色素P450酶系统/分离和提纯大肠杆菌/酶学大肠杆菌/遗传学血红素/化学铁/化学氧合酶类/化学氧合酶类/遗传学氧合酶类/分离和提纯重组蛋白质类/化学重组蛋白质类/遗传学重组蛋白质类/分离和提纯硫化叶菌属/酶学硫化叶菌属/遗传学

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Biochemical characterization of the Hjc Holliday junction resolvase of Pyrococcus furiosus

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NUCLEIC ACIDS RESEARCH 2000年第22期28卷 4544-4551页

作者： Komori, K Sakae, S Fujikane, R Morikawa, K Shinagawa, H Ishino, Y BERI Dept Mol Biol Suita Osaka 5650874 Japan BERI Dept Biol Struct Suita Osaka 5650874 Japan Osaka Univ Microbial Dis Res Inst Dept Mol Microbiol Suita Osaka 5650871 Japan

The Hjc protein of Pyrococcus furiosus is an endonuclease that: resolves Holliday junctions, the intermediates in homologous recombination, The amino acid sequence of Hjc is conserved in Archaea, however, it is not-similar to any of the well-characterized Holliday junction resolvases, In order to investigate the similarity and diversity of the enzymatic properties of Hjc as a Holliday junction resolvase, highly purified Hjc produced in recombinant Escherichia coli was used for detailed: biochemical characterizations. Hjc has specific binding activity to the Holliday-structured DNA, with an apparent dissociation constant (K-d) of 60 nan, The dimeric form of Hjc binds to the substrate DMA. The optimal reaction conditions were determined using a synthetic Holliday junction as substrate, Hjc required a divalent cation for cleavage activity and Mg2+ at 5-10 mM was optimal, Mn2+ could substitute for Mg2+, but it was much less efficient than Mg2+ as the cofactor. The cleavage reaction was stimulated by alkaline pH and KCI at similar to 200 mM, In addition to the high specific activity, Hjc was found to be extremely heat stable, In contrast to the case of Sulfolobus, the Holliday:junction resolving activity detected in *** cell extract thus far is only derived from Hjc.

关键词：古细菌蛋白质类/遗传学古细菌蛋白质类/分离和提纯古细菌蛋白质类/代谢阳离子二价/药理学 DNA/化学 DNA/遗传学 DNA/代谢脱氧核糖核酸酶类位点特异性Ⅱ型/遗传学脱氧核糖核酸酶类位点特异性Ⅱ型/分离和提纯脱氧核糖核酸酶类位点特异性Ⅱ型/代谢内切脱氧核糖核酸酶类/遗传学内切脱氧核糖核酸酶类/分离和提纯内切脱氧核糖核酸酶类/代谢酶稳定性霍利迪连结体解离酶类氢离子浓度动力学镁/药理学锰/药理学核酸构象氯化钾/药理学蛋白质结合/药物作用火球菌属/酶学底物特异性

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Archaeal genomics

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CURRENT OPINION IN MICROBIOLOGY 1999年第5期2卷 542-547页

作者： Gaasterland, T Rockefeller Univ Lab Computat Genet New York NY 10021 USA

Four euryarchaeal genomes have been completely sequenced and are publicly available: Methanococcus jannaschii, Methanobacterium thermoautotrophicum, Pyrococcus horikoshii and Archaeoglobus fulgidus. Four more genome sequences, two crenarchaeal and two pyrococci, will soon be released. In addition, seven more archaeal genome sequencing projects are under way, including two halophiles, two Thermoplasma, and a methanogen. These projects cover all branches of the archaeal domain and will lead to new insights into archaeal metabolism, DNA processing, and evolutionary relationships with the Bacteria and Eukarya.

关键词：古细菌/分类古细菌/遗传学古细菌/代谢古细菌蛋白质类/化学古细菌蛋白质类/遗传学古细菌蛋白质类/分离和提纯 DNA 古细菌/化学 DNA 古细菌/遗传学 DNA 古细菌/代谢基因组古细菌种系发生蛋白质组序列分析 DNA

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