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

R Aparicio; E V Eneiskaya; A A Kulminskaya; A N Savel'ev; A M Golubev; K N Neustroev; J Kobarg; I Polikarpov

doi:10.1107/s0907444999016625

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

Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):342-3. doi: 10.1107/s0907444999016625.

Authors

R Aparicio¹, E V Eneiskaya, A A Kulminskaya, A N Savel'ev, A M Golubev, K N Neustroev, J Kobarg, I Polikarpov

Affiliation

¹ National Synchrotron Light Laboratory, LNLS, Caixa Postal 6192, CEP 13083-970, Campinas, SP, Brazil.

PMID: 10713521
DOI: 10.1107/s0907444999016625

Abstract

beta-Mannosidase from Trichoderma reesei, a 105 kDa glycoprotein, has been crystallized. The crystals belong to the space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell dimensions a = b = 165.86, c = 122.46 A, and diffract beyond 2.75 A resolution. X-ray diffraction data were collected from a frozen crystal on a synchrotron X-ray source.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Crystallography, X-Ray
Fungal Proteins / chemistry*
Fungal Proteins / isolation & purification
Mannosidases / chemistry*
Mannosidases / isolation & purification
Models, Molecular
Protein Conformation
Trichoderma / enzymology*
beta-Mannosidase

Substances

Fungal Proteins
Mannosidases
beta-Mannosidase