| Research Abstract |
An in-house system for X-ray intensity data collection from bio-macromolecular crystals was developed. The system consists of a new X-ray detector(RAXIS-IV)and an improved fine focused(0.1 mm x 1.0 mm)X-ray generator(FR-C). Using two large(300 mm x 300 mm)imaging plates, the detector was designed to yield a short read-out time with high sensitivity. The X-ray beam was focused with Supper's double-mirror. The system was used for data collections of several protein-DNA complex protein-ligand complex and protein-protein crystals and structure determinations of these crystals were performed using the intensity data obtained. These are the mouse transcription factor IRF-2 complexed with DNA, the fission yeast transcription factor Papl complexed with DNA, mouse hippocampal serine protease neuropsin, the human small G protein RhoA in the GTP γS-Mg^<2+> bound form and its complex with the effector protein PKN, and the mouse radixin FERM domain in the free, IP3-bound, and ICAM-2-bound forms.
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