Preliminary crystallographic analysis of sweet potato beta amylase.
Beta amylase from sweet potato has been crystallized in a form suitable for high resolution X-ray diffraction analysis from a mixture of polyethylene glycol 400 and ammonium sulfate at room temperature. The crystals are rectangular prisms and occasionally reach a size of 1 mm on an edge. The space group of the crystals is I422 with cell dimensions of a = b = 196.4 A and c = 72.2 A. There are four tetramers of about M(r) = 210,000 in the unit cell centered at 222 symmetry points. The asymmetric unit is a single beta amylase subunit of about M(r) = 52,000. The tetrameric molecule must have exact 222 molecular symmetry relating its subunits.
Cudney
R
R
Department of Biochemistry, University of California at Riverside 92521.
McPherson
A
A
D003460:Crystallization; D010944:Plants / Q000201:enzymology; D014961:X-Ray Diffraction; D001614:beta-Amylase / Q000737:chemistry*
D001614:beta-Amylase