Crystallization and preliminary X-ray crystallographic analysis of the soybrean proglycinin expressed in Escherichia coli.
Glycinin is one of the dominant storage proteins of soybean seeds. Soybean proglycinin expressed in Escherichia coli has been crystallized from Tris.HCl buffer (pH 7.6) by the dialysis equilibrium method. The crystals belong to the tetragonal system, space group P4(1) or P4(3), with unit cell dimensions of a = b = 115.2 A, and c = 147.1 A. The asymmetric unit contains three molecules of proglycinin, with crystal volume per protein mass (Vm) of 3.05 A3/Da and solvent content of 58.4% by volume. The crystals diffract X-rays to a resolution limit of at least 2.9 A and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis.
Research Institute for Food Science, Kyoto University, Japan.
S
S
Utsumi
A B
AB
Gidamis
B
B
Mikami
M
M
Kito
D004926:Escherichia coli / Q000235:genetics; D005916:Globulins / Q000737:chemistry* / Q000235:genetics; D011498:Protein Precursors / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry; D030262:Soybean Proteins; D013025:Glycine max / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D005916:Globulins; D011498:Protein Precursors; D011994:Recombinant Proteins; D030262:Soybean Proteins; C011474:glycinin