Crystallization and preliminary diffraction data of Escherichia coli ADP glucose pyrophosphorylase.
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.
Mulichak
A M
AM
Department of Chemistry, Michigan State University, East Lansing 48824.
Skrzypczak-Jankun
E
E
Rydel
T J
TJ
Tulinsky
A
A
Preiss
J
J
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D051599:Glucose-1-Phosphate Adenylyltransferase; D009713:Nucleotidyltransferases / Q000302:isolation & purification; D014961:X-Ray Diffraction
D009713:Nucleotidyltransferases; D051599:Glucose-1-Phosphate Adenylyltransferase