Crystallization and preliminary X-ray study of β-­mannosidase from Trichoderma reesei

Crystallization and preliminary X-ray study of β-­mannosidase from Trichoderma reesei

β‐Mannosidase from Trichoderma reesei, a 105 kDa glycoprotein, has been crystallized. The crystals belong to the space group P41212 or P43212, with unit‐cell dimensions a = b = 165.86, c = 122.46 Å, and diffract beyond 2.75 Å resolution. X‐ray diffraction data were collected from a frozen crystal on...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2000-03, Vol.56 (3), p.342-343
Hauptverfasser: Aparicio, R., Eneiskaya, E. V., Kulminskaya, A. A., Savel'ev, A. N., Golubev, A. M., Neustroev, K. N., Kobarg, J., Polikarpov, I.
Format: Artikel
Sprache:eng
Schlagworte:
beta-Mannosidase
Crystallization
Crystallography, X-Ray
Fungal Proteins - chemistry
Fungal Proteins - isolation & purification
Mannosidases - chemistry
Mannosidases - isolation & purification
Models, Molecular
Protein Conformation
Trichoderma - enzymology
β-mannosidase
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Zusammenfassung:β‐Mannosidase from Trichoderma reesei, a 105 kDa glycoprotein, has been crystallized. The crystals belong to the space group P41212 or P43212, with unit‐cell dimensions a = b = 165.86, c = 122.46 Å, and diffract beyond 2.75 Å resolution. X‐ray diffraction data were collected from a frozen crystal on a synchrotron X‐ray source.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444999016625