TY - JOUR
T1 - Crystallization and preliminary X-ray studies of two serine proteinase inhibitors, BGIA and BGIT from the seeds of bitter gourd
AU - Kondo, Hidemasa
AU - Nakanose, Jin
AU - Nakagawa, Atsushi
AU - Tanaka, Isao
AU - Kimura, Makoto
AU - Funatsu, Gunki
N1 - Funding Information:
We thank Professor N. Sakabe and Drs. N. Watanabe and M. Suzuki for their help in data collection at the Photon Factory, High Energy Physics Laboratory, Japan. This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan. A.N. and I.T. are members of the TARA project.
PY - 1997/11
Y1 - 1997/11
N2 - 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.
AB - 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.
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U2 - 10.1006/jsbi.1997.3931
DO - 10.1006/jsbi.1997.3931
M3 - Article
C2 - 9417986
AN - SCOPUS:0031456307
SN - 1047-8477
VL - 120
SP - 204
EP - 206
JO - Journal of Structural Biology
JF - Journal of Structural Biology
IS - 2
ER -