Výsledky vyhledávání - "Hélène Souchon"

Crystal structures of pheasant and guinea fowl egg-white lysozymes

Autor: J. Lescar, Hélène Souchon, Pedro M. Alzari

Publikováno v: Protein Science. 3:788-798

The crystal structures of pheasant and guinea fowl lysozymes have been determined by X-ray diffraction methods. Guinea fowl lysozyme crystallizes in space group P6(1)22 with cell dimensions a = 89.2 A and c = 61.7 A. The structure was refined to a fi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9206dfee257770b6809fa11f308f6c21
https://doi.org/10.1002/pro.5560030508

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Bound water molecules and conformational stabilization help mediate an antigen-antibody association

Autor: W. Dall'Acqua, Roy A. Mariuzza, Hélène Souchon, Mark I. Greene, Graham A. Bentley, G. Boulot, Roberto J. Poljak, Talapady N. Bhat, D Tello, F P Schwarz

Publikováno v: Proceedings of the National Academy of Sciences. 91:1089-1093

We report the three-dimensional structures, at 1.8-A resolution, of the Fv fragment of the anti-hen egg white lysozyme antibody D1.3 in its free and antigen-bound forms. These structures reveal a role for solvent molecules in stabilizing the complex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa61622c5e3fa95e47b2ee3a57d7794b
https://doi.org/10.1073/pnas.91.3.1089

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Crystallization of a family 8 cellulase from Clostridium thermocellum

Autor: Pierre Béguin, Pedro M. Alzari, Hélène Souchon

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 25:134-136

The catalytic domain of cellulase CelA, a family 8 glycohydrolase from C. thermocellum, has been crystallized in the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a = 50.12 A, b = 63.52 A, c = 104.97 A. The diffraction pattern exte

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a2099edcb143c91fd5ab033fcf41e98e
https://doi.org/10.1002/(sici)1097-0134(199605)25:1<134::aid-prot12>3.0.co

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Crystal structure of an anti-carbohydrate antibody directed against Vibrio cholerae O1 in complex with antigen: Molecular basis for serotype specificity

Autor: P.-s. Lei, Jean-Michel Fournier, C. P. J. Glaudemans, P. Kováč, S. Villeneuve, Pedro M. Alzari, Jean-Claude Mazie, Hélène Souchon, M.-M. Riottot

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2000, 97 (15), pp.8433-8438. ⟨10.1073/pnas.060022997⟩
Proceedings of the National Academy of Sciences of the United States of America, 2000, 97 (15), pp.8433-8438. ⟨10.1073/pnas.060022997⟩

International audience; The crystal structure of the murine Fab S-20-4 from a protective anti-cholera Ab specific for the lipopolysaccharide Ag of the Ogawa serotype has been determined in its unliganded form and in complex with synthetic fragments o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30515ab373d6d00d5048f58e9432da4f
https://hal-pasteur.archives-ouvertes.fr/pasteur-03144732

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Crystallization of a family 8 cellulase from Clostridium thermocellum

Autor: Hélène Souchon, Pierre Béguin, Pedro M. Alzari

Publikováno v: Proteins-Structure, Function and Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, 1996, 25 (1), pp.134-136. ⟨10.1002/(SICI)1097-0134(199605)25:13.0.CO;2-L⟩
Proteins-Structure, Function and Bioinformatics, 1996, 25 (1), pp.134-136. ⟨10.1002/(SICI)1097-0134(199605)25:13.0.CO;2-L⟩

International audience; The catalytic domain of cellulase CelA, a family 8 glycohydrolase from C. thermocellum, has been crystallized in the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a = 50.12 A, b = 63.52 A, c = 104.97 A. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80f6ccf0fa01918f93e114dcf86cdd58
https://hal-pasteur.archives-ouvertes.fr/pasteur-03136610

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The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism

Autor: Roberto Dominguez, Pedro M. Alzari, Marie Bernard Lascombe, Hélène Souchon

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, 1996, 257 (5), pp.1042-1051. ⟨10.1006/jmbi.1996.0222⟩
Journal of Molecular Biology, Elsevier, 1996, 257 (5), pp.1042-1051. ⟨10.1006/jmbi.1996.0222⟩

International audience; The structures of the Glu140-->Gln mutant of the Clostridium thermocellum endoglucanase CelC in unliganded form (CelC(E140Q)) and in complex with cellohexaose (CelC(E140Q)-Gl(C6)) have been refined to crystallographic R-factor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4d58ad70b600576875c331256e42a79
https://pubmed.ncbi.nlm.nih.gov/8632467

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Structural and Functional Analysis of the Metal-binding Sites of Clostridium thermocellum Endoglucanase CelD

Autor: Patrick Chariot, Pierre Béguin, Hélène Souchon, Pedro M. Alzari, Sylvie Chauvaux

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, 1995, 270 (17), pp.9757-9762. ⟨10.1074/jbc.270.17.9757⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1995, 270 (17), pp.9757-9762. ⟨10.1074/jbc.270.17.9757⟩

International audience; Crystallographic analysis indicated that Clostridium thermocellum endoglucanase CelD contained three Ca(2+)-binding sites, termed A, B, and C, and one Zn(2+)-binding site. The protein contributed five, six, and three of the co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59a758712fc518c2e9cf6db581a6d347
https://hal-pasteur.archives-ouvertes.fr/pasteur-03136564/file/1-s2.0-S0021925817474850-main.pdf

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Multiple crystal forms of endoglucanase CelD: signal peptide residues modulate lattice formation

Autor: Pedro M. Alzari, Pierre Béguine, Silvia Spinelli, Hélène Souchon, V. Chitarra, Michel Juy

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 1995, 248 (2), pp.225-232. ⟨10.1016/S0022-2836(95)80045-X⟩
Journal of Molecular Biology, 1995, 248 (2), pp.225-232. ⟨10.1016/S0022-2836(95)80045-X⟩
Scopus-Elsevier

International audience; The crystal structure of Clostridium thermocellum endoglucanase CelD revealed an extended NH2-terminal segment (involving residues from the putative leader peptide) sticking out from the enzyme core to interact with a symmetry

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::031f21a6c231fb89fa05cf36fb8349d0
https://hal.archives-ouvertes.fr/hal-00314460

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Characterization of two crystal forms of Clostridium thermocellum endoglucanase CelC

Autor: Pedro M. Alzari, Roberto Dominguez, Hélène Souchon

Publikováno v: Proteins: Structure, Function, and Genetics
Proteins: Structure, Function, and Genetics, Wiley, 1994, 19 (2), pp.158-160. ⟨10.1002/prot.340190209⟩
Proteins: Structure, Function, and Genetics, 1994, 19 (2), pp.158-160. ⟨10.1002/prot.340190209⟩

International audience; Endoglucanase CelC from Clostridium thermocellum expressed in Escherichia coli has been crystallized in two different crystal forms by the hanging drop method. Crystals of form I were grown with polyethylene glycol as a precip

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3539a4799d255926e19d7b745c00e814
https://pubmed.ncbi.nlm.nih.gov/8090710

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