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Crystallization and preliminary X-ray crystallographic analysis of recombinant beta-mannosidase from Aspergillus niger
Autoři | |
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Rok publikování | 2013 |
Druh | Konferenční abstrakty |
Fakulta / Pracoviště MU | |
Citace | |
Popis | 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. |
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