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Expression, purification and preliminary X-ray crystallographic analysis of PsaA, a putative metal-transporter protein of Streptococcus pneumoniae

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1998年第6-2期54卷 1464-1466页

作者： Pilling, PA Lawrence, MC Berry, AM Ogunniyi, AD Lock, RA Paton, JC Biomol Res Inst Parkville Vic 3052 Australia Womens & Childrens Hosp Mol Microbiol Unit Adelaide SA 5006 Australia

The putative metal-transporter protein PsaA of Streptococcus pneumoniae is of potential interest both as a vaccine and also as a drug target. The overexpression of the protein in E. coti, and its subsequent purification and crystallization are described. The crystals are rectangular rods and diffract to beyond 2.7 Angstrom resolution. The crystal space group is P2(1)2(1)2(1) with unit-cell dimensions a = 59.9, b = 66.5 and c = 69.9 Angstrom.

关键词：黏着素细菌细菌蛋白质类载体蛋白质类/生物合成载体蛋白质类/化学载体蛋白质类/遗传学载体蛋白质类/分离和提纯克隆分子结晶结晶学 X线大肠杆菌脂蛋白类/生物合成脂蛋白类/化学脂蛋白类/遗传学脂蛋白类/分离和提纯膜转运蛋白质类重组融合蛋白质类/生物合成重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯肺炎链球菌/化学肺炎链球菌/遗传学

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Crystallization and preliminary X-ray diffraction studies of 6-phosphogluconate dehydrogenase from Lactococcus lactis

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1998年第6-2期54卷 1422-1424页

作者： Tetaud, E Hall, DR Gourley, DG Leonard, GA Arkison, S Barrett, MP Hunter, WN Univ Dundee Dept Biochem Dundee DD1 4HN Scotland Joint Struct Biol Grp ESRF F-38043 Grenoble France Univ Glasgow Inst Biomed & Life Sci Dept Biochem Parasitol Glasgow G12 8QQ Lanark Scotland

6-Phosphogluconate dehydrogenase is one of the seven enzymes involved in the pentose phosphate pathway. Crystals of a mammalian and a protozoan enzyme have been obtained previously and structures determined. It is reported here that a bacterial fi-phosphogluconate dehydrogenase, from Lactococcus lactis, has been purified and used in crystallization trials. Large prisms suitable for a detailed structural analysis have been obtained and characterized as orthorhombic, space group F222, with a = 70.4, b = 105.7, c = 474.6 Angstrom. Diffraction has been observed to 2.2 Angstrom resolution using synchrotron radiation. Structural analysis, in combination with ongoing biochemical characterization, will assist the elucidation of the structure-activity relationships of this enzyme.

关键词：细菌蛋白质类/化学细菌蛋白质类/分离和提纯结晶结晶学 X线二聚作用乳乳球菌/酶学磷酸戊糖途径磷酸葡糖脱氢酶/化学磷酸葡糖脱氢酶/分离和提纯蛋白质构象重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯

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Crystallization and preliminary X-ray studies of the Rhizobium meliloti DctD two-component receiver domain

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ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 1998年第6-2期54卷 1416-1418页

作者： Staley, M Zeringue, LC Kidd, RD Nixon, BT Farber, GK Penn State Univ Dept Biochem & Mol Biol 108 Althouse Lab University Pk PA 16802 USA

The Rhizobium meliloti DctD two-component receiver domain was expressed in Escherichia coli and purified to homogeneity. Crystals were obtained using the hanging-drop vapor-diffusion geometry with ammonium phosphate as the precipitant. The crystals diffract to 2.3 Angstrom and exhibit the symmetry of space group I222 or I2(1)2(1)2(1). The unit-cell dimensions are a = 59.0, b = 58.6 and c = 169.8 Angstrom. The asymmetric unit contains a dimer and the crystals have a V-m of 2.16 Angstrom(3) Da(-1).

关键词：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线蛋白质构象重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯信号传导苜蓿中华根瘤菌/化学苜蓿中华根瘤菌/遗传学转录因子/化学转录因子/遗传学转录因子/分离和提纯

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Crystallization of ovine placental lactogen in a 1:2 complex with the extracellular domain of the rat prolactin receptor

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1998年第6-2期54卷 1408-1411页

作者： Christinger, HW Elkins, PA Sandowski, Y Sakal, E Gertler, A Kossiakoff, AA de Vos, AM Genentech Inc Dept Prot Engn S San Francisco CA 94080 USA Hebrew Univ Jerusalem Inst Biochem Food Sci & Nutr Fac Agr IL-76100 Rehovot Israel

Growth hormone and prolactin control somato-lactogenic biology. While high-resolution crystal structures have been determined for receptor complexes of human growth hormone, no such information exists for prolactin. A stable 1:2 complex was formed between ovine placental lactogen, a close prolactin homologue, and two copies of the extracellular portion of the rat prolactin receptor. Using synchrotron radiation, native data have been collected to 2.3 Angstrom. Crystals contain one complex per asymmetric unit. The crystal structure of this complex will shed light on the structural reasons for cross-reactivity and specificity among the endocrine hormones, placental lactogen, prolactin and growth hormone.

关键词：结晶结晶学 X线大分子物质胎盘催乳激素/化学胎盘催乳激素/分离和提纯胎盘催乳激素/代谢催乳素/化学蛋白质构象受体催乳素/化学受体催乳素/代谢重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯绵羊动物大鼠

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Production, crystallization and diffraction to atomic resolution of an antibody Fv specific for the blood-group A oligosaccharide antigen

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1998年第6-2期54卷 1456-1459页

作者： Patenaude, SI MacKenzie, CR Bilous, D To, RJ Ryan, SE Young, NM Evans, SV Univ Ottawa Dept Biochem Ottawa ON K1H 8M5 Canada Natl Res Council Canada Inst Biol Sci Ottawa ON K1A 0R6 Canada

The histoblood-group ABO carbohydrate antigens are well known as important factors in blood transfusions, but they can also act as receptors for infectious agents and have been implicated in susceptibility to certain carcinomas. A single-chain variable-domain antigen-binding fragment (scFv) gene based on the known sequence of an anti-blood-group-A monoclonal antibody (AC1001) has been synthesized and expressed in Escherichia coti. The purified scFv preparation existed primarily in the monomeric form but also contained large amounts of dimeric and higher oligomeric forms. The corresponding variable-domain antigen-binding fragment (Fv) was generated by cleaving the V-L-V-H linker with subtilisin, and its activity was demonstrated by surface plasmon resonance with an immobilized bovine serum albumin A-trisaccharide conjugate (K-D = 290 mu M). AC1001 Fv crystals grown in the presence of N-acetylgalactosamine diffracted to 0.93 Angstrom resolution. This is the first reported example of a crystal of an antibody antigen-binding fragment diffracting to atomic resolution.

关键词： ABO血型系统/免疫学乙酰半乳糖胺/化学乙酰半乳糖胺/免疫学抗原抗体复合物/化学碳水化合物序列克隆分子结晶结晶学 X线血凝素类/化学血凝素类/遗传学血凝素类/分离和提纯免疫球蛋白碎片/化学免疫球蛋白碎片/遗传学免疫球蛋白碎片/分离和提纯分子序列数据寡糖类/免疫学寡糖类/代谢重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯血清白蛋白牛表面等离激元动物牛

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Crystallization and preliminary X-ray diffraction study of lactonohydrolase from Fusarium oxysporum

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1998年第6-2期54卷 1432-1434页

作者： Kataoka, M Yamamoto, K Shimizu, S Ohta, M Kita, A Higuchi, Y Miki, K Kyoto Univ Grad Sch Agr Div Appl Life Sci Sakyo Ku Kyoto 6068502 Japan Kyoto Univ Grad Sch Sci Dept Chem Sakyo Ku Kyoto 6068502 Japan

The lactonohydrolase from the fungus Fusarium oxysporum AKU 3702 was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 4000 as a precipitant. The crystals belong to the monoclinic space group P2(1) with unit-cell parameters a = 156, b = 100, c = 94.1 Angstrom, beta = 91.7 degrees. Assuming that there are two lactonohydrolase-dimer molecules in the asymmetric unit, the crystal volume per unit molecular mass. V-m, is calculated to be 2.94 Angstrom(3) Da(-1).

关键词：羧酸酯水解酶类/化学羧酸酯水解酶类/分离和提纯结晶结晶学 X线真菌蛋白质类/化学真菌蛋白质类/分离和提纯镰刀菌属/酶学分子量蛋白质构象重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯

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Crystallization of two related lectins from the legume plant Dolichos biflorus

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ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 1998年第6-2期54卷 1446-1449页

作者： Dao-Thi, MH Hamelryck, TW Bouckaert, J Korber, F Burkow, V Poortmans, F Etzler, M Strecker, G Wyns, L Loris, R Free Univ Brussels VIB Lab Ultrastruct B-1640 Rhode St Genese Belgium Liverpool John Moores Univ Liverpool L3 3AF Merseyside England Univ Tromso Dept Chem N-900 Tromso Norway Vlaamse Instelling Technol Onderzoek B-2400 Mol Belgium Univ Calif Davis Sect Mol & Cellular Biol Davis CA 95616 USA Univ Sci & Tech Lille Flandres Artois F-59655 Villeneuve Dascq France

The seed lectin DBL and the related stem and leaves lectin DB58 of the tropical legume Dolichos biflorus were crystallized, as well as complexes of DBL with adenine and with GalNAc(alpha 1-3)[Fuc(alpha 1-2)]Gal. The d... 详细信息

关键词：腺嘌呤/代谢碳水化合物序列结晶结晶学 X线外源凝集素类/化学外源凝集素类/分离和提纯外源凝集素类/代谢大分子物质分子序列数据寡糖类/代谢植物凝集素类受体有丝分裂原/代谢重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯重组融合蛋白质类/代谢

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Bacillus subtilis regulatory protein GerE

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ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 1998年第6-2期54卷 1453-1455页

作者： Ducros, VMA Brannigan, JA Lewis, RJ Wilkinson, AJ Univ York Dept Chem York YO10 5DD N Yorkshire England

GerE is the latest-acting of a series of factors which regulate gene expression in the mother cell during sporulation in Bacillus. The gene encoding GerE has been cloned from B. subtilis and overexpressed in Escherichia coli. Purified GerE has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. The small plate-like crystals belong to the monoclinic space group C2 and diffract beyond 2.2 Angstrom resolution with a synchrotron radiation X-ray source.

关键词：枯草芽孢杆菌/化学枯草芽孢杆菌/生理学细菌蛋白质类/化学克隆分子结晶结晶学 X线电泳聚丙烯酰氨凝胶重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯 ∑因子孢子细菌转录因子

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Crystallization and preliminary crystallographic study of tropinone reductase II from Datura stramonium

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1998年第6-2期54卷 1405-1407页

作者： Yamashita, A Nakajima, K Kato, H Hashimoto, T Yamada, Y Oda, J Kyoto Univ Chem Res Inst Uji Kyoto 611011 Japan Nara Inst Sci & Technol Grad Sch Biol Sci Nara 630010 Japan

Tropinone reductase II is an NADPH-dependent oxidoreductase involved in a plant alkaloid metabolism. The enzyme from Datura stramonium has been crystallized using 2-methyl-2,4-pentanediol as a precipitant and a macro-seeding technique. The crystal belongs to space group P4(2)2(1)2, with cell dimensions a = b = 62.8 Angstrom and c = 128.4 Angstrom. A data set to 2.6 Angstrom resolution has been collected at a cryogenic temperature.

关键词：醇氧化还原酶类/化学醇氧化还原酶类/分离和提纯结晶结晶学 X线模型分子植物蛋白质类/化学植物蛋白质类/分离和提纯植物有毒/酶学蛋白质构象重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯

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Crystallization and preliminary X-ray studies of a recombinant calcium-binding protein from Entamoeba histolytica

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1998年第6-2期54卷 1442-1445页

作者： Gopal, B Suma, R Murthy, MRN Bhattacharya, A Bhattacharya, S Indian Inst Sci Mol Biophys Unit Bangalore 560012 Karnataka India Jawaharlal Nehru Univ Sch Life Sci New Delhi 110067 India Jawaharlal Nehru Univ Sch Environm Sci New Delhi 110067 India

A calcium-binding protein (CaBP) of Entamoeba histolytica was purified from an E. coli recombinant clone carrying the CaBP gene in a pET-3c expression vector using anion-exchange and size-exclusion chromatography. Examination of the amino-acid sequence of the recombinant protein suggested that it has four independent EF-hand motifs. The protein dissolved in cacodylate buffer was crystallized using the hanging-drop method with 2-methylpentane-2,4-diol (MPD) as the precipitant. X-ray diffraction data have been collected on these crystals using a MAR Research imaging-plate detector system attached to a Rigaku RU200 rotating-anode X-ray generator. The crystals belong to the hexagonal space group P6(1)22 with unit-cell dimensions of a = b = 96.21, c = 65.48 Angstrom. Preliminary molecular-replacement computations suggest that the structure of this protein is likely to be similar to that of calmodulin (CAM).

关键词：氨基酸序列钙结合蛋白质类/化学钙结合蛋白质类/分离和提纯结晶结晶学 X线黑腹果蝇/化学溶组织内阿米巴/化学模型分子分子序列数据分子量蛋白质构象原虫蛋白质类/化学原虫蛋白质类/分离和提纯重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯序列比对序列同源性氨基酸种特异性动物

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