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Crystallization and preliminary diffraction data of Escherichia coli ADP glucose pyrophosphorylase
A M Mulichak1, E Skrzypczak-Jankun, T J Rydel
1Department of Chemistry, Michigan State University, East Lansing 48824.
The Journal of Biological Chemistry
|November 25, 1988
Abstract:
ADP glucose pyrophosphorylase from Escherichia coli has been crystallized from polyethylene glycol 8000 solutions. The crystals are: orthorhombic, a = 155(2), b = 153(2), c = 174(2) A, space group P2(1)2(1)2(1), four tetrameric molecules/unit cell. This gives a solvent fraction of about 75% consistent with the relatively poor diffraction quality of crystals (5.0-A resolution) and their sensitivity to x-ray exposure damage. Ways of circumventing the former and improving the latter are proposed.