Crystallization of the catalytic domain of Clostridium cellulolyticum CeLF cellulase in the presence of a newly synthesized cellulase inhibitor

Autor: Reverbel-Leroy, C., Parsiegla, G., Moreau, V., Juy, M., Tardif, C., Driguez, H., Belaich, J.P., Haser, R.

Publikováno v: Acta Crystallogr. Sect. D-Biol. Crystallogr.
Acta Crystallogr. Sect. D-Biol. Crystallogr., 1998, pp.114-118

The catalytic domain of the CeIF processive endocellulase, a family 48 glycosyl hydrolase from Clostridium cellulolyticum has been crystallized in the presence of a newly synthesized inhibitor (methyl 4-S-beta-cellobiosyl-4-thio-beta-cellobioside), b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::b61c7d5fb3458fce4a7294bc68fc01a9
https://hal.archives-ouvertes.fr/hal-00313560

Purification and characterization of endoglucanase C from Clostridium cellulolyticum. Catalytic comparison with endoglucanase A

Autor: Fierobe, H.P., Bagnara-Tardif, C., Gaudin, C., Guerlesquin, F., Sauve, P., Belaich, A., Belaich, J.P.

Publikováno v: European Journal of Biochemistry
European Journal of Biochemistry, Wiley, 1993, 217, pp.557
European Journal of Biochemistry, 1993, 217, pp.557

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::0163a21005f2d4296e60a8f5d112bcb9
https://hal.archives-ouvertes.fr/hal-00320702

(Study on the β-galactoside permease of Escherichiacoli) solubilization of a thiodigalactoside-binding protein from E. colimembrane containing β-galactoside permease

Autor: Belaich, A., Simonpietri, P., Belaich, J.P.

Publikováno v: Biochemical and Biophysical Research Communications; June 1978, Vol. 82 Issue: 3 p847-852, 6p

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