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A simple method for the isolation and purification of L-asparaginase from Enterobacter aerogenes

FOLIA MICROBIOLOGICA 1999年第1期44卷 15-18页

作者： Mukherjee, J Joeris, K Riechel, P Scheper, T Univ Hannover Inst Chem Tech D-30167 Hannover Germany

L-Asparaginase from Enterobacter aerogenes was purified by a simple method involving sonication of the crude cell mass, gel filtration with Sephacryl S-100 as the separating material, followed by ultrafiltration. Recent methods involve complex purification procedures of 5-6 steps. The isolation process resulted in 10-fold purification of the enzyme with a specific activity of 55 IU/mg protein and recovery of 54 %. The purity was tested by capillary electrophoresis, used for the first time for documenting the purification of l-asparaginase. The choice of the column material was critical in the purification process.

关键词：天冬酰胺酶/分离和提纯细菌蛋白质类/分离和提纯色谱法凝胶肠杆菌属/化学超声处理超滤

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Purification, crystallization and preliminary X-ray analysis of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa

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ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 1999年第9期55卷 1591-1593页

作者： Sainz, G Vicat, J Kahn, R Tricot, C Stalon, V Dideberg, O Inst Biol Struct JP Ebel CNRS CEA Lab Cristallog Macromol F-38027 Grenoble 1 France Free Univ Brussels Fac Sci Inst Rech Microbiol JM Wiame Microbiol Lab B-1070 Brussels Belgium

The catabolic ornithine carbamoyltransferase (OTCase) from Pseudomonas aeruginosa exhibits allosteric behaviour, with two conformational states of the molecule: an active R form and an inactive T form. The enzyme is a dodecamer with a molecular mass of 455 700 Da. Three crystal forms have been obtained. Crystals of allosteric state Tare rhombohedral, belonging to the R3 space group, with hexagonal unit-cell parameters a = b = 180.6, c = 122.0 Angstrom. They diffract to a resolution of 4.5 Angstrom. Two crystal forms for allosteric state R have been obtained, with hexagonal and cubic symmetries. Hexagonal crystals, which diffract to a resolution of 3.4 Angstrom, belong to the space group P6(3) with unit-cell parameters a = b = 140.8, c = 145.6 Angstrom. The cubic crystals belong to space group I23, with unit-cell parameter a = 134.32 Angstrom and diffract to a resolution better than 2.5 Angstrom. In all crystal forms, the dodecamer exhibits a 23 point-group symmetry.

关键词：细菌蛋白质类/化学细菌蛋白质类/分离和提纯细菌蛋白质类/代谢催化作用结晶结晶学 X线鸟氨酸氨甲酰转移酶/化学鸟氨酸氨甲酰转移酶/分离和提纯鸟氨酸氨甲酰转移酶/代谢蛋白质构象铜绿假单胞菌/酶学

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Antibacterial peptide from H-pylori

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NATURE 1999年第6729期398卷 671-672页

作者： Pütsep, K Brändén, CI Boman, HG Normark, S Karolinska Inst Ctr Microbiol & Tumor Biol SE-17177 Stockholm Sweden

Colonization of the human stomach by the bacterium Helicobacter pylori is a predisposing factor for gastrointestinal illnesses such as gastritis and peptic ulcers. But most infections are asymptomatic, and it has recently been suggested that H. pylori may actually have beneficial effects on infected carriers who are heavily exposed to other gastrointestinal pathogens. We find that H. pylori possesses antibacterial activity to which it is itself resistant. We have traced this activity to cecropin-like amino-terminal peptides derived from the ribosomal protein L1 (RpL1).

关键词：氨基酸序列抗菌药/化学抗菌药/分离和提纯抗菌药/药理学芽孢杆菌巨大/药物作用细菌蛋白质类/化学细菌蛋白质类/分离和提纯细菌蛋白质类/药理学大肠杆菌/药物作用螺杆菌感染螺杆菌幽门/化学肽类核糖体蛋白质类/分离和提纯胃/微生物学人类

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Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1999年第5期55卷 1046-1047页

作者： Newberry, KJ Kohn, J Hou, YM Perona, JJ Univ Calif Santa Barbara Dept Chem Santa Barbara CA 93106 USA Univ Calif Santa Barbara Interdepartmental Program Biochem & Mol Biol Santa Barbara CA 93106 USA Thomas Jefferson Univ Dept Biochem & Mol Pharmacol Philadelphia PA 19107 USA

Crystals of the 52 kDa monomeric Escherichia coli cysteinyl-tRNA synthetase complexed with ATP and cysteine have been grown by hanging-drop vapor diffusion from solutions containing ammonium sulfate as the precipitating agent. The crystals form long hexagonal rods in the space group P321 with unit-cell dimensions a = b = 82.3, c = 168.9 Angstrom. There is one enzyme molecule in the asymmetric unit. A complete native data set has been collected from a rotating-anode source to a resolution of 2.7 Angstrom at 103 K, with an R-merge of 6.7%.

关键词：氨酰基tRNA合成酶类/化学氨酰基tRNA合成酶类/分离和提纯细菌蛋白质类/化学细菌蛋白质类/分离和提纯结晶结晶学 X线大肠杆菌/酶学蛋白质构象

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Crystallization of the regulatory and effector domains of the key sporulation response regulator Spo0A

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ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 1999年第Pt 3期55卷 671-676页

作者： Muchová, K Lewis, RJ Brannigan, JA Offen, WA Brown, DP Barák, I Youngman, P Wilkinson, AJ Slovak Acad Sci Inst Mol Biol Bratislava 84251 Slovakia Univ York Dept Chem York YO10 5DD N Yorkshire England Univ Georgia Dept Genet Athens GA 30602 USA

The key response-regulator gene of sporulation, spo0A, has been cloned from Bacillus stearothermophilus and the encoded protein purified. The DNA-binding and phospho-acceptor domains of Spo0A have been prepared by tryptic digestion of the intact protein and subsequently crystallized in forms suitable for X-ray crystallographic studies. The DNA-binding domain has been crystallized in two forms, one of which diffracts X-rays to beyond 2.5 Angstrom spacing. The crystals of the phospho-acceptor domain diffract X-rays beyond 2.0 Angstrom spacing using synchrotron radiation.

关键词：氨基酸序列细菌蛋白质类/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线嗜热脂肪芽孢杆菌/遗传学水解作用分子序列数据蛋白质构象序列同源性氨基酸转录因子/化学转录因子/遗传学转录因子/分离和提纯

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Expression of the csp protein family upon cold shock and production of tetracycline in Streptomyces aureofaciens

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BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 1999年第2期265卷 305-310页

作者： Mikulík, K Khanh-Hoang, Q Halada, P Bezousková, S Benada, O Bêhal, V Acad Sci Czech Republ Inst Microbiol CR-14220 Prague 4 Czech Republic

A shift down in temperature causes in Streptomyces aureofaciens a transient repression of polypeptide synthesis. During the acclimation phase 32 proteins were synthesized. The addition of tetracycline (200 mu g/ml) to cells from exponential phase of growth leads to induction of 27 novel proteins and 17 upregulated proteins migrated in 2-D gel as proteins expressed upon cold shock. Immunoblot analysis using antibodies raised against CspB, CspC, and CspD of Bacillus subtilis revealed five cross-reactive proteins of the Csp family. Proteins CspB and CspD are predominantly induced at low temperature or by the presence of tetracycline. Expression of Csp proteins during the acclimation phase is regulated on the transcription level. Proteins of the Csp family have been shown to be associated with ribosomes and can be removed by 1 M. NH,CI. As expression of Csp proteins differs during development or temperature shift down, these proteins can be considered as trans-acting factors to form contacts with the coding region of specific mRNAs. (C) 1999 Academic Press.

关键词：氨基酸序列细菌蛋白质类/生物合成细菌蛋白质类/遗传学细菌蛋白质类/分离和提纯冷基因表达调控细菌热休克蛋白质类/生物合成热休克蛋白质类/遗传学动力学 RNA 细菌/遗传学 RNA 细菌/代谢 RNA 信使/遗传学 RNA 信使/代谢核糖体/代谢链霉菌生金/遗传学链霉菌生金/生长和发育链霉菌生金/代谢四环素/生物合成四环素/药理学

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Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the receiver domain of PhoB

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ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 1998年第6-2期54卷 1460-1463页

作者： Sola, M Gomis-Ruth, FX Guasch, A Serrano, L Coll, M CSIC Cid Dept Mol & Cellular Biol Ctr Invest & Desenvolupament ES-08034 Barcelona Spain European Mol Biol Lab D-69117 Heidelberg Germany

PhoB is the response regulator of the E. coli two-component signal transduction system for phosphate regulation. It is a transcription factor that activates more than 30 genes of the pho regulon. Crystals of the receiver domain of PhoB were obtained by applying the hanging-drop vapour-diffusion method. X-ray diffraction data have been collected using synchrotron radiation to 1.88 Angstrom resolution. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell constants a = 34.11, b = 60.42, c = 119.97 Angstrom. The Matthews parameter suggests that PhoB crystallizes with two molecules per asymmetric unit, suggesting that activating dimerization occurs in the crystal.

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/分离和提纯结晶结晶学 X线大肠杆菌/化学大肠杆菌/遗传学膜蛋白质类/化学重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯转录因子/化学转录因子/遗传学转录因子/分离和提纯

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Purification and preliminary X-ray crystallographic studies of recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1998年第6-2期54卷 1397-1398页

作者： Kack, H Gibson, KJ Gatenby, AA Schneider, G Lindovist, Y Karolinska Inst Dept Med Biochem & Biophys Div Mol Struct Biol S-17177 Stockholm Sweden Dupont Co Cent Res & Dev Expt Stn Wilmington DE 19880 USA

Recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli, a pyridoxal-phosphate-dependent amino-transferase, has been crystallized in space groups P2(1) and C2. Both crystal forms were obtained at pH 7.3 with 21% polyethylene glycol and 10% 2-propanol as precipitants. The cell dimensions were a = 130, b = 57.5, c = 117 Angstrom, beta = 110 degrees for the C2 crystals, and a = 58.4, b = 55.6, c = 121 Angstrom, beta = 96.9 degrees for the P21 crystals, which diffract to at least 2.6 and 2.0 Angstrom resolution, respectively.

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线大肠杆菌/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/分离和提纯转氨酶类/化学转氨酶类/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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Preliminary crystallographic studies of triosephosphate isomerase (TIM) from the hyperthermophilic Archaeon Pyrococcus woesei

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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 1998年第6-2期54卷 1419-1421页

作者： Bell, GS Russell, RJM Kohlhoff, M Hensel, R Danson, MJ Hough, DW Taylor, GL Univ Bath Dept Biol & Biochem Ctr Extremophile Res Bath BA2 7AY Avon England Univ Essen Gesamthsch D-45117 Essen Germany

Recombinant triosephosphate isomerase (TIM) from a hyperthermophilic Archaeon, Pyrococcus woesei, has been crystallized. Three crystal forms have been obtained: monoclinic, orthorhombic and hexagonal. The monoclinic crystals belong to space group P2(1) with cell dimensions a = 79.1, b = 89.2, c = 145.4 Angstrom and beta = 92.8 degrees, and diffract to at least 2.6 Angstrom. The orthorhombic crystals belong to space group P2(1)2(1)2 with a = 89.4, b = 155.9, c = 79.5 Angstrom, and diffract to 2.9 Angstrom. Diffraction from the hexagonal form showed extensive disorder. The monoclinic form contains two tetramers in the asymmetric unit, which are in the same orientation but related by a pseudo-centring. The orthorhombic form contains one tetramer in the asymmetric unit which is in approximately the same orientation as in the monoclinic form. Knowledge of the structure of this hyperthermostable TIM, which is tetrameric in contrast to dimeric forms previously observed, will add to the understanding of protein thermostability.

关键词：细菌蛋白质类/化学细菌蛋白质类/分离和提纯生物聚合物克隆分子结晶结晶学 X线大肠杆菌蛋白质构象焦球菌属/酶学重组融合蛋白质类/化学重组融合蛋白质类/分离和提纯丙糖磷酸异构酶/化学丙糖磷酸异构酶/分离和提纯

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