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Titolo:
Crystallization and preliminary X-ray crystallographic analysis of NAD(+)-dependent DNA ligase from Thermus filiformis
Autore:
Lee, JY; Kim, HK; Chang, CS; Eom, SH; Hwang, KY; Cho, YJ; Yu, YG; Ryu, SE; Kwon, ST; Suh, SW;
Indirizzi:
Seoul Natl Univ, Coll Nat Sci, Dept Chem, Div Chem & Mol Engn, Seoul 151742, South Korea Seoul Natl Univ Seoul South Korea 151742 Engn, Seoul 151742, South Korea Sung Kyun Kwan Univ, Dept Genet Engn, Suwon 440746, South Korea Sung Kyun Kwan Univ Suwon South Korea 440746 , Suwon 440746, South Korea Kwangju Inst Sci & Technol, Dept Life Sci, Kwangju 500712, South Korea Kwangju Inst Sci & Technol Kwangju South Korea 500712 00712, South Korea Korea Adv Inst Sci & Technol, Struct Biol Ctr, Seoul 136791, South Korea Korea Adv Inst Sci & Technol Seoul South Korea 136791 36791, South Korea KIST, Korea Res Inst Biosci & Biotechnol, Div Prot Engn, Taejon 305600, South Korea KIST Taejon South Korea 305600 Div Prot Engn, Taejon 305600, South Korea
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 56, anno: 2000,
parte:, 3
pagine: 357 - 358
SICI:
0907-4449(200003)56:<357:CAPXCA>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
12
Recensione:
Indirizzi per estratti:
Indirizzo: Suh, SW Seoul Natl Univ, Coll Nat Sci, Dept Chem, Div Chem & Mol Engn, Seoul 151742, South Korea Seoul Natl Univ Seoul South Korea 151742 oul 151742, South Korea
Citazione:
J.Y. Lee et al., "Crystallization and preliminary X-ray crystallographic analysis of NAD(+)-dependent DNA ligase from Thermus filiformis", ACT CRYST D, 56, 2000, pp. 357-358

Abstract

A highly thermostable DNA ligase from Thermus filiformis has been crystallized at room temperature using methoxypolyethylene glycol 5000 as a precipitant. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 90.63, b = 117.80, c = 98.65 Angstrom, beta = 115.56 degrees. Two molecules of DNA ligase are present in the asymmetric unit, givinga crystal volume per protein mass (V-m) of 3.1 Angstrom(3) Da(-1) and a solvent content of 61%. A native data set extending to 3.0 Angstrom resolution has been collected at 100 K using synchrotron X-rays.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 10:31:59