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Crystallization of the A-domain of the mannitol transport protein enzyme IImtl.

作者信息

Lammers L A, Dijkstra B W, van Weeghel R P, Pas H H, Robillard G T

机构信息

BIOSON Research Institute, University of Groningen, The Netherlands.

出版信息

J Mol Biol. 1992 Nov 5;228(1):310-2. doi: 10.1016/0022-2836(92)90511-h.

Abstract

The A-domain of the mannitol transport protein enzyme IImtl from Escherichia coli (relative molecular mass 16,300) was crystallized, both at room temperature and 4 degrees C, from 40% polyethylene glycol 6000 (pH 8.5 to 9.0) using the hanging-drop method of vapour diffusion. The crystals have the monoclinic space group P2(1), with unit cell dimensions a = 54.0 A, b = 67.0 A, c = 80.9 A and beta = 100.8 degrees. They diffract to 2.6 A resolution. A self-rotation function and self-Patterson suggest that there are four molecules in the asymmetric unit showing mmm symmetry.

摘要

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