Development of X-ray intensity data-collection system for macromolecular crystals

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An instrument system for X-ray intensity data collection from bio-macromolecular crystals in a laboratory 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 oil and vacuum sealing of the X-ray generator was improved to yield long-lasting seals. The X-ray beam was focused with Supper's double-mirror. The system was used for data collections of several protein-DNA complex, protein-GTP complex and protein crystals and structure determinations of these crystals were performed using the intensity data obtained. These are the budding yeast transcription factor PHO4 complexed with DNA,the mouse transcription factor IRF-2 complexed with DNA,the fission yeast transcription factor Pap1 complexed with DNA,mouse hippocampal serine protease neuropsin, the human small G protein RhoA complexed with GTPgammaS,the human small G protein RhoA complexed with GTPgammaS,the HPt domain of a E.coli sensor kinase ArcB complexed with a E.coli response regulator CheY,the HPt domain of ArcB a E.coli phospho-histidine phosphatase SixA.