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  • Title: Crystallization and preliminary X-ray studies of two serine proteinase inhibitors, BGIA and BGIT, from the seeds of bitter gourd.
    Author: Kondo H, Nakanose J, Nakagawa A, Tanaka I, Kimura M, Funatsu G.
    Journal: J Struct Biol; 1997 Nov; 120(2):204-6. PubMed ID: 9417986.
    Abstract:
    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.
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