Crystallization of a scRIP-gelonin isolated from plant seeds Gelonium multiforum.
Single crystals of the protein gelonin isolated from the seeds of Gelonium multiforum have been grown at room temperature by vapor diffusion method. The crystals are monclinic with a = 49.4 A, b = 44.9 A, c = 137.4 A, and beta = 98.3 degrees. The space group is P2(1), with two molecules in the asymmetric unit which are related by a noncrystallographic 2-fold axis along psi = 13 degrees and phi = 88 degrees. The crystals diffract X-rays to high resolution, making it possible to obtain an accurate structure of this single chain ribosome inactivating protein.
Satyamurthy
P
P
Solid State Physics Division, Bhabha Atomic Research Centre, Trombay, Bombay, India.
Hosur
M V
MV
Misquith
S
S
Surolia
A
A
Kannan
K K
KK
D018360:Crystallography, X-Ray; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D011500:Protein Synthesis Inhibitors / Q000737:chemistry*; D054789:Ribosome Inactivating Proteins, Type 1; D012639:Seeds / Q000737:chemistry*
D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D054789:Ribosome Inactivating Proteins, Type 1; C025674:GEL protein, Gelonium multiflorum