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See detailCrystallization of ornithine acetyltransferase from yeast by counter-diffusion and preliminary X-ray study
Maes, D.; Crabeel, M.; Van de Weerdt, Cécile ULg et al

in Acta Crystallographica Section F-Structural Biology and Crystallization Communications (2006), 62(Part 12), 1294-1297

A study is presented on the crystallization of ornithine acetyltransferase from yeast, which catalyzes the fifth step in microbial arginine synthesis. The use of the counter-diffusion technique removes ... [more ▼]

A study is presented on the crystallization of ornithine acetyltransferase from yeast, which catalyzes the fifth step in microbial arginine synthesis. The use of the counter-diffusion technique removes the disorder present in one dimension in crystals grown by either the batch or hanging-drop techniques. This makes the difference between useless crystals and crystals that allow successful determination of the structure of the protein. The crystals belong to space group P4, with unit-cell parameters a = b = 66.98, c = 427.09 angstrom, and a data set was collected to 2.76 angstrom. [less ▲]

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See detailCrystallization of vitreous high-T-c superconducting oxide through laser zone melting method.
Ausloos, Marcel ULg; Bougrine, Hassan ULg; Cloots, Rudi ULg et al

in Institute of Physics Conference Series (1995), 148

We synthesized Bi2Sr2CaCu2O8-y ceramics through the vitreous route. After insertion in epoxy resin, we exposed the materials to a CO2 laser beam. Various intensities and sweeping conditions were examined ... [more ▼]

We synthesized Bi2Sr2CaCu2O8-y ceramics through the vitreous route. After insertion in epoxy resin, we exposed the materials to a CO2 laser beam. Various intensities and sweeping conditions were examined. We observed the samples in high resolution polarized light microscopy and with electron scanning microscopy. Crystallization zones could be detected. A systematic analysis gave the correlation between the behavior of the material and its synthesis conditions. Electrical properties were measured through micro-electrode deposited on the surface at various locations. No superconductivity was found. The optimization of such a process and potential applications will be discussed. [less ▲]

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See detailCrystallization sequence and magma chamber processes in the ferrobasaltic Sept Iles layered intrusion, Canada
Namur, Olivier ULg; Charlier, Bernard ULg; Toplis, Michael et al

in Journal of Petrology (2010), 51

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See detailCrystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound to IQ motifs from myosin V
Terrak, Mohammed ULg; Otterbein, L. R.; Wu, G. et al

in Acta Crystallographica Section D-Biological Crystallography (2002), 58(Pt 10 Pt 2), 1882-5

Mlc1p is a calmodulin-like protein from the budding yeast Saccharomyces cerevisiae, where it has been identified as a subunit of a class V myosin, Myo2p, and a binding partner of an IQGAP-like protein ... [more ▼]

Mlc1p is a calmodulin-like protein from the budding yeast Saccharomyces cerevisiae, where it has been identified as a subunit of a class V myosin, Myo2p, and a binding partner of an IQGAP-like protein, Iqg1p. Through its interactions with these two proteins, Mlc1p plays a role in polarized growth and cytokinesis. Mlc1p has been crystallized in complexes with four different IQ target motifs from the neck region of Myo2p: IQ2, IQ3, IQ4 and IQ2-IQ3 (referred to as IQ2,3). Electron-density maps for two of the complexes (Mlc1p-IQ4 and Mlc1p-IQ2,3) were obtained from multiple anomalous dispersion (MAD) experiments based on selenomethionine derivatives. The other two structures (Mlc1p-IQ2 and Mlc1p-IQ3) were determined by molecular replacement using the partially refined structure of Mlc1p-IQ2,3 as a search model. [less ▲]

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See detailCrystallographic analysis of family 11 endo-beta-1,4-xylanase Xyl1 from Streptomyces sp. S38.
Wouters, J.; Georis, J.; Engher, D. et al

in Acta Crystallographica Section D-Biological Crystallography (2001), 57(Pt 12), 1813-9

Family 11 endo-beta-1,4-xylanases degrade xylan, the main constituent of plant hemicelluloses, and have many potential uses in biotechnology. The structure of Xyl1, a family 11 endo-xylanase from ... [more ▼]

Family 11 endo-beta-1,4-xylanases degrade xylan, the main constituent of plant hemicelluloses, and have many potential uses in biotechnology. The structure of Xyl1, a family 11 endo-xylanase from Streptomyces sp. S38, has been solved. The protein crystallized from ammonium sulfate in the trigonal space group P321, with unit-cell parameters a = b = 71.49, c = 130.30 A, gamma = 120.0 degrees. The structure was solved at 2.0 A by X-ray crystallography using the molecular-replacement method and refined to a final R factor of 18.5% (R(free) = 26.9%). Xyl1 has the overall fold characteristic of family 11 xylanases, with two highly twisted beta-sheets defining a long cleft containing the two catalytic residues Glu87 and Glu177. [less ▲]

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See detailCrystallographic data for a penicillin receptor : exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61
Knox, James R.; DeLucia, Mary L.; Murthy, N. S. et al

in Journal of Molecular Biology (1979), 127(2), 217-218

A pencillin-sensitive enzyme, the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61, has been crystallized from polyethylene glycol (Mr = 6000 to 7500) solution at pH 7•6. X-ray ... [more ▼]

A pencillin-sensitive enzyme, the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61, has been crystallized from polyethylene glycol (Mr = 6000 to 7500) solution at pH 7•6. X-ray examination of the orthorhombic crystals shows the space group is P212121, with unit cell dimensions a = 51•1 Å, B = 67•4 Å, and C = 102•9 Å. With four molecules of molecular weight 38,000, the Å3/dalton ratio for the cell is 2•33. The crystals are stable to irradiation for 75 hours and are suitable for structure analysis to at least 2•4 Å resolution. The radius of gyration of the molecule in solution at pH 6.8 is 20.8 Å. [less ▲]

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See detailCrystallographic data for the beta-lactamase from Enterobacter cloacae P99.
Charlier, Paulette ULg; Dideberg, O.; Frère, Jean-Marie ULg et al

in Journal of Molecular Biology (1983), 171(2), 237-8

The beta-lactamase from Enterobacter cloacae P99 has been crystallized from polyethylene glycol solution at pH 7. X-ray examination of the orthorhombic crystals shows the space group is P2(1)2(1)2 with ... [more ▼]

The beta-lactamase from Enterobacter cloacae P99 has been crystallized from polyethylene glycol solution at pH 7. X-ray examination of the orthorhombic crystals shows the space group is P2(1)2(1)2 with unit cell dimensions a = 77.4 A, b = 69.4 A, and c = 63.6 A. There is one molecule of molecular weight 39,000 in the asymmetric unit. [less ▲]

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See detailCrystallographic data for the DD-carboxypeptidase-endopeptidase of low penicillin sensitivity excreted by Streptomyces albus g
Dideberg, Otto; Frère, Jean-Marie ULg; Ghuysen, Jean-Marie ULg

in Journal of Molecular Biology (1979), 129(4), 677-679

The DD-carboxypeptidase-endopeptidase of low penicillin sensitivity that is excreted by Streptomyces albus G has been crystallized from a polyethylene glycol (Mr 6000 to 7500) solution at pH 8.0. X-ray ... [more ▼]

The DD-carboxypeptidase-endopeptidase of low penicillin sensitivity that is excreted by Streptomyces albus G has been crystallized from a polyethylene glycol (Mr 6000 to 7500) solution at pH 8.0. X-ray examination of the prismatic crystals shows that the space group is P21 with unit cell dimensions a = 51.1 Å, B = 49.7 Å, C = 38.7 Å, β = 100.6 ° and one molecule in the asymmetric unit. A crystal suspension made in 50 mM -Tris • HCl buffer (pH 8.0) supplemented with 5 mM-MgCl2 and 16% (w/v) polyethylene glycol exhibits enzyme activity on the substrate Ac2-L-Lys-D-Ala-D-Ala. [less ▲]

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See detailCrystallographic mapping of β-lactams bound to a D-alanyl-D-alanine peptidase target enzyme
Kelly, Judith A.; Knox, James R.; Zhao, Haiching C. et al

in Journal of Molecular Biology (1989), 209(2), 281-295

X-ray crystallography has been used to examine the binding of three members of the beta-lactam family of antibiotics to the D-alanyl-D-alanine peptidase from Streptomyces R61, a target of penicillins ... [more ▼]

X-ray crystallography has been used to examine the binding of three members of the beta-lactam family of antibiotics to the D-alanyl-D-alanine peptidase from Streptomyces R61, a target of penicillins. Cephalosporin C, the monobactam analog of penicillin G and (2,3)-alpha-methylene benzylpenicillin have been mapped at 2.3 A resolution in the form of acyl-enzyme complexes bound to serine 62. On the basis of the positions of these inhibitors, the binding of a tripeptide substrate for the enzyme, L-lysyl-D-alanyl-D-alanine, has been modeled in the active site. The binding of both inhibitors and substrate is facilitated by hydrogen-bonding interactions with a conserved beta-strand (297-303), which is antiparallel to the beta-lactam's acylamide linkage or the substrate's peptide bond. The active site is similar to that in beta-lactamases. [less ▲]

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See detailCrystallographic studies of low penicillin-sensitive enzyme excreted by Streptomyces albus G [proceedings]
Dideberg, O.; Charlier, Paulette ULg

in Archives Internationales de Physiologie et de Biochimie (1979), 87(5), 1045

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See detailThe CSDP Olympiad from a Scientific Point of View
Paile, Sylvain ULg

in Zambas, Symeon (Ed.) The 1st Common Security and Defence Policy Olympiad (2013)

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See detailCSL TV chambers Updating
Grodent, Christophe ULg; franco

Conference (2006)

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See detailCSR Performance Measurements: Motivations, Tools and Survey Results
Crutzen, Nathalie ULg

Scientific conference (2010, December 02)

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See detailCT findings of an intra-abdominal metastatic sertoli cell tumor in a dog
Taylor, Olivia; Hamaide, Annick ULg; Mercier, Elise ULg et al

Poster (2013, December 01)

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See detailCT SCAN FEATURES OF PRESUMPTIVE HAEMORRHAGIC STROKE IN A DOG WITH CUSHING’S DISEASE
Liotta, Annalisa Pia ULg; Cavrenne, Romain; Peeters, Dominique ULg et al

in Case reports in Veterinary Medicine (in press)

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See detailCTD measurements, with emphasis on Elephant Island surroundings
Dauby, Patrick ULg

in Berichte zur Polar- und Meeresforschung (2003), 470

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See detailCTIP2 is a negative regulator of P-TEFb.
Cherrier, Thomas ULg; Le Douce, Valentin; Eilebrecht, Sebastian et al

in Proceedings of the National Academy of Sciences of the United States of America (2013), 110(31), 12655-60

The positive transcription elongation factor b (P-TEFb) is involved in physiological and pathological events including inflammation, cancer, AIDS, and cardiac hypertrophy. The balance between its active ... [more ▼]

The positive transcription elongation factor b (P-TEFb) is involved in physiological and pathological events including inflammation, cancer, AIDS, and cardiac hypertrophy. The balance between its active and inactive form is tightly controlled to ensure cellular integrity. We report that the transcriptional repressor CTIP2 is a major modulator of P-TEFb activity. CTIP2 copurifies and interacts with an inactive P-TEFb complex containing the 7SK snRNA and HEXIM1. CTIP2 associates directly with HEXIM1 and, via the loop 2 of the 7SK snRNA, with P-TEFb. In this nucleoprotein complex, CTIP2 significantly represses the Cdk9 kinase activity of P-TEFb. Accordingly, we show that CTIP2 inhibits large sets of P-TEFb- and 7SK snRNA-sensitive genes. In hearts of hypertrophic cardiomyopathic mice, CTIP2 controls P-TEFb-sensitive pathways involved in the establishment of this pathology. Overexpression of the beta-myosin heavy chain protein contributes to the pathological cardiac wall thickening. The inactive P-TEFb complex associates with CTIP2 at the MYH7 gene promoter to repress its activity. Taken together, our results strongly suggest that CTIP2 controls P-TEFb function in physiological and pathological conditions. [less ▲]

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