Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Crystallization, preliminary X-ray analysis of a native and selenomethionine D-hydantoinase from Thermus sp.
Autore:
Abendroth, J; Niefind, K; Chatterjee, S; Schomburg, D;
Indirizzi:
Univ Cologne, Inst Biochem, D-50674 Cologne, Germany Univ Cologne Cologne Germany D-50674 t Biochem, D-50674 Cologne, Germany
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 56, anno: 2000,
parte:, 9
pagine: 1166 - 1169
SICI:
0907-4449(200009)56:<1166:CPXAOA>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
5-SUBSTITUTED HYDANTOINS; ENZYMATIC PRODUCTION; AMINO-ACIDS; PROTEINS; MAD;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
17
Recensione:
Indirizzi per estratti:
Indirizzo: Schomburg, D Univ Cologne, Inst Biochem, Zulpicher Str 47, D-50674 Cologne, Germany Univ Cologne Zulpicher Str 47 Cologne Germany D-50674 ermany
Citazione:
J. Abendroth et al., "Crystallization, preliminary X-ray analysis of a native and selenomethionine D-hydantoinase from Thermus sp.", ACT CRYST D, 56, 2000, pp. 1166-1169

Abstract

A D-hydantoinase from Thermus sp. was expressed in Escherichia coli, purified to homogeneity and crystallized both as native and Se-Met labelled protein. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 125.9, b = 215.8, c = 207.5 Angstrom. A three-wavelength MAD data set was collected to 2.5 Angstrom resolution and a native data set was collected to 1.7 Angstrom resolution. Crystal packing and self-rotation calculations led to the assumption of six protomers per asymmetric unit, corresponding to a V-M value of 2.28 Angstrom(3) Da(-1) and a solvent content of 46%. As each protomer contains nine Se-Met residues, 54 selenium sites per asymmetric unit were present and could be unambigously located in the course of the MAD experiment. This selenium substructure is one of the largest selenium substructures that have been solved to date. The resultingphases obtained at a high-resolution limit of 3.0 Angstrom could be extended to 1.7 Angstrom and refined by application of density-modification techniques, especially non-crystallographic symmetry.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 07:00:26