http://www.cnr.it/ontology/cnr/individuo/prodotto/ID240373
Structure of Sulfur-Substituted Rhodanese at 1.36 Å Resolution (Articolo in rivista)
- Type
- Label
- Structure of Sulfur-Substituted Rhodanese at 1.36 Å Resolution (Articolo in rivista) (literal)
- Anno
- 1998-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1107/S090744499701216X (literal)
- Alternative label
Francesca Gliubich ab, Rodolfo Berni c, Marcello Colapietro d, Luisa Barba e, Giuseppe Zanotti a (1998)
Structure of Sulfur-Substituted Rhodanese at 1.36 Å Resolution
in Acta crystallographica. Section D, Biological crystallography.; Blackwell, Oxford (Regno Unito)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Francesca Gliubich ab, Rodolfo Berni c, Marcello Colapietro d, Luisa Barba e, Giuseppe Zanotti a (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://scripts.iucr.org/cgi-bin/paper?S090744499701216X (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Scopu (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- a Department of Organic Chemistry, University of Padova and Biopolymer Research Center, CNR, 35131, Padova, Italy,
b Institute of Pharmaceutical Chemistry, University of Milano, 20135 Milano, Italy,
c Institute of Biochemical Sciences, University of Parma, 43100 Parma, Italy,
d Department of Chemistry, University of Rome `La Sapienza', 00185 Roma, Italy
e Centro di Strutturistica Chimica `G. Giacomello', Sezione di Trieste, 34012 Trieste, Italy. (literal)
- Titolo
- Structure of Sulfur-Substituted Rhodanese at 1.36 Å Resolution (literal)
- Abstract
- 1.36 Å resolution X-ray diffraction data have been recorded at 100 K for bovine liver sulfur-substituted rhodanese, using synchrotron radiation. The crystal structure has been refined anisotropically to a final R factor of 0.159 (Rfree = 0.229) for 53 034 unique reflections. The model contains 2 327 protein atoms and 407 solvent molecules, with a good geometry. The high resolution allows full details for helices, [beta]-sheets, tight turns and of all inter- and intramolecular interactions stabilizing the enzyme molecule to be given. The situation at the active site is described, particularly in regard to the network of hydrogen bonds made by S[gamma] and S[delta] of the sulfur-substituted catalytic Cys247 and surrounding groups and solvent molecules. The replacement of the precipitant ammonium sulfate with cryoprotectants in the crystal-suspending medium led to the removal of the sulfate ion from the enzyme active site. Only limited changes of the enzyme structure have been found as a result of the drastic change in the crystal medium. (literal)
- Editore
- Prodotto di
- Autore CNR
Incoming links:
- Autore CNR di
- Prodotto
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
- Editore di