Crystallization and preliminary X-ray crystallographic analysis of recombinant beta-mannosidase from Aspergillus niger

Investor logo
Investor logo

Warning

This publication doesn't include Faculty of Education. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.
Authors

DEMO Gabriel FLIEDROVA Barbora WEIGNEROVA Lenka WIMMEROVÁ Michaela

Year of publication 2013
Type Conference abstract
MU Faculty or unit

Central European Institute of Technology

Citation
Description We report the crystallization and preliminary X-ray crystallographic analysis of recombinant beta-mannosidase overexpressed in Pichia pastoris. The best crystals were produced by further optimization using the hanging-drop vapour diffusion method. Diffraction data were collected at BESSY II Berlin (14.1 and 14.2). The data were processed by XDSAPP. The crystals belonged to space group P1. The beta-mannosidase in the native data set diffracted to 2.41 A resolution. Experimental phasing, model fitting and refinement are in progress.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.