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Volumn 6, Issue 5, 2008, Pages 851-853

Probing the β-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; MOLECULAR STRUCTURE; OLIGOSACCHARIDES;

EID: 43249124256     PISSN: 14770520     EISSN: None     Source Type: Journal    
DOI: 10.1039/b719288f     Document Type: Article
Times cited : (5)

References (25)
  • 16
    • 0030293109 scopus 로고    scopus 로고
    • Crystals of CtLic26A were grown as previously from 0.15 M ammonium sulfate, 30% PEG 5 K MME 0.1 M MES pH 6.5 and ∼10 mM compound 1. Data, to 1.5 A resolution, were collected on beamline ID14-3 of the European Synchrotron Radiation Source. Data reduction and all subsequent processing involved the CCP4 suite (Collaborative Computational Project Number 4, Acta Crystallogr., 1994, D50, 760-763), with structure solution performed with AMoRE -1855
    • V. Moreau J. L. Viladot E. Samain A. Planas H. Driguez Bioorg. Med. Chem. 1996 4 1849 1855
    • (1996) Bioorg. Med. Chem. , vol.4 , pp. 1849
    • Moreau, V.1    Viladot, J.L.2    Samain, E.3    Planas, A.4    Driguez, H.5
  • 20
    • 0030729838 scopus 로고    scopus 로고
    • Site directed variants were made as described previously.2 Enzyme kinetics were measured both against high viscosity β-glucan (Megazyme, Eire) through detection of reducing sugars using the dinitrosalicylic acid method -134
    • R. M. Esnouf J. Mol. Graphics Modell. 1997 15 132 134)
    • (1997) J. Mol. Graphics Modell. , vol.15 , pp. 132
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.