http://www.cnr.it/ontology/cnr/individuo/prodotto/ID244175
Crystallization and preliminary X-ray diffraction of the endopoligalatturonase from Fusarium moniliforme (Articolo in rivista)
- Type
- Label
- Crystallization and preliminary X-ray diffraction of the endopoligalatturonase from Fusarium moniliforme (Articolo in rivista) (literal)
- Anno
- 1999-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1107/S0907444999005454 (literal)
- Alternative label
Federici, L; Mattei, B; Caprari, C; Savino, C; Cervone, F; Tsernoglou, D (1999)
Crystallization and preliminary X-ray diffraction of the endopoligalatturonase from Fusarium moniliforme
in Acta crystallographica. Section D, Biological crystallography.; MUNKSGAARD INT PUBL LTD, COPENHAGEN (Danimarca); Wiley-Blackwell Publishing, Inc., Malden (Stati Uniti d'America)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Federici, L; Mattei, B; Caprari, C; Savino, C; Cervone, F; Tsernoglou, D (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- [ 1 ] CNR, Dipartimento Sci Biochim, I-00185 Rome, Italy
[ 2 ] CNR, Ctr Mol Biol, I-00185 Rome, Italy
[ 3 ] Univ Rome La Sapienza, Dipartimento Biol Vegetale, I-00185 Rome, Italy (literal)
- Titolo
- Crystallization and preliminary X-ray diffraction of the endopoligalatturonase from Fusarium moniliforme (literal)
- Abstract
- Endo-polygalacturonases catalyze the fragmentation and solubilization of the homogalacturonan of the plant cell wan. These enzymes are extracellularly targeted glycoproteins produced by a number of organisms such as fungi, bacteria and plants, and are involved in both pathological and physiological processes. Single crystals of the endopolygalacturonase from the phytopathogenic fungus Fusarium moniliforme were obtained by the vapour-diffusion method at 294 K. The starting material as well as the crystal consist of three forms with different degrees of glycosylation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) and diffract to 1.9 Angstrom resolution on a synchrotron-radiation source under cryocooling conditions. (literal)
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