Crystallization and preliminary X-ray studies of two serine proteinase inhibitors, BGIA and BGIT from the seeds of bitter gourd

Hidemasa Kondo, Jin Nakanose, Atsushi Nakagawa, Isao Tanaka, Makoto Kimura, Gunki Funatsu

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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 Å, b = 23.7 Å, c = 47.9 Å, and β = 105.4°, and diffracted X-ray up to 1.5 Å resolution. Crystals of BGIT belong to the triclinic space group P1 with cell dimensions of a = 22.8 Å, b = 23.5 Å, c = 28.4 Å, α = 93.1°, β = 99.6°, and γ = 101.0°, giving X-ray diffraction of over 1.2 Å resolution. Intensity data of BGIA and BGIT crystals were collected using synchrotron radiation up to 1.7 and 1.4 Å, respectively.

Original languageEnglish
Pages (from-to)204-206
Number of pages3
JournalJournal of structural biology
Volume120
Issue number2
DOIs
Publication statusPublished - Nov 1997

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All Science Journal Classification (ASJC) codes

  • Structural Biology

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