Crystallization and preliminary x-ray crystallographic studies of trichosanthin delta C7 |
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| Authors: | Li X Ding Y Wang Z Liu Yi Dong Y Shaw P Rao Z Too H |
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| Affiliation: | Laboratory of Structural Biology and the MOE Laboratory of Protein Science, School of Life Science & Engineering, Tsinghua University, Beijing 100084, China. |
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| Abstract: | Trichosanthin (TCS) is a type I ribosome-inactivating protein (RIP) which possesses rRNA N-glycosidase activity. TCS has various pharmacological properties. It is possible to reduce the antigenicity of TCS by deleting up to seven C-terminal residues of TCS (TCS-C7) with minimal effect on its activity. TCS-C7 has been crystallized and the crystal diffracted to 1.8 A. It belongs to space group P2(1), with unit-cell parameters a=71.6A, b=74.4A, c=87.6A, beta=97.0 degrees. It is given that there are four molecules per asymmetric unit. |
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