Crystallization and preliminary X-ray crystallographic study of ribosome-inactivating protein from barley seeds.
Ribosome-inactivating protein from barley seeds has been crystallized using polyethylene glycol as precipitant. The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 88.36, b = 62.59, c = 53.18 A and beta = 108.62 degrees. The asymmetric unit contains one molecule of ribosome-inactivating protein with a corresponding crystal volume per protein mass (V(m)) of 2.32 A(3) Da(-1) and a solvent content of 47% by volume. The crystal diffracts to about 2.3 A with X-rays from a rotating-anode source and is very stable in the X-ray beam. X-ray data (nearly complete to 2.4 A Bragg spacing) have been collected from a native crystal.
Song
H K
HK
Department of Chemistry, College of Natural Sciences, Seoul National University, Korea.
Hwang
K Y
KY
Kim
K K
KK
Suh
S W
SW