Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds.
Large crystals of probable amylase/protease inhibitor-B have been grown at room temperature from ammonium sulfate solution. The crystals grow within five days to dimensions of 0.6 mm x 0.6 mm x 0.6 mm. They diffract to at least 1.7 A upon exposure to synchrotron X-rays. The crystals belong to the space group P4(1)2(1)2 (or P4(3)2(1)2) with unit cell dimensions of a = 38.02 A and c = 98.98 A. The presence of one molecule per asymmetric unit gives the unit cell volume per protein mass (Vm) of 1.99 A3/Da and the solvent fraction of 38.2% by volume. X-ray data have been collected to 2.0 A Bragg spacing from native crystals.
Hwang
K Y
KY
Department of Chemistry, College of Natural Sciences Seoul National University, Korea.
Kim
K K
KK
Min
K
K
Eom
S H
SH
Yu
Y G
YG
Kim
S
S
Sweet
R M
RM
Suh
S W
SW
D003460:Crystallization; D012275:Oryza / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011480:Protease Inhibitors / Q000737:chemistry; D014961:X-Ray Diffraction; D000516:alpha-Amylases / Q000037:antagonists & inhibitors
D010940:Plant Proteins; D011480:Protease Inhibitors; C079243:probable amylase-protease inhibitor-B, Oryza sativa; D000516:alpha-Amylases