Crystallization and preliminary X-ray studies of two serine proteinase inhibitors, BGIA and BGIT, from the seeds of bitter gourd.
Two serine proteinase inhibitors from seeds of the bitter gourd, BGIA (bitter gourd inhibitor against acidic amino acid-specific proteinase of Streptomyces griseus) and BGIT (bitter gourd trypsin inhibitor), were crystallized for X-ray structure determination. Crystals of BGIA belong to the monoclinic space group C2 with cell dimensions of a = 54.0 A, b = 23.7 A, c = 47.9 A, and beta = 105.4 degrees, and diffracted X-ray up to 1.5 A resolution. Crystals of BGIT belong to the triclinic space group P1 with cell dimensions of a = 22.8 A, b = 23.5 A, c = 28.4 A, alpha = 93.1 degrees, beta = 99.6 degrees, and gamma = 101.0 degrees, giving X-ray diffraction of over 1.2 A resolution. Intensity data of BGIA and BGIT crystals were collected using synchrotron radiation up to 1.7 and 1.4 A, respectively.
Kondo
H
H
Graduate School of Science, Hokkaido University, Sapporo, 060, Japan.
Nakanose
J
J
Nakagawa
A
A
Tanaka
I
I
Kimura
M
M
Funatsu
G
G
D003460:Crystallization; D018360:Crystallography, X-Ray; D019662:Cucurbitaceae / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012639:Seeds / Q000737:chemistry; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000302:isolation & purification
D010455:Peptides; D010940:Plant Proteins; D015842:Serine Proteinase Inhibitors; D014361:Trypsin Inhibitors; C093459:trypsin inhibitor BGIT, Momordica charantia; C070697:BGIA protease inhibitor