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Recently, high brilliance and highly focused synchrotron beam lines, X-ray data collection at low temperature and technical advances in crystallographic analysis have significantly improved the resolution of X-ray crystallography. Crystallization in microgravity environment is one of the potential techniques for improving quality of protein crystals. In this study Takaamylase, a member of alpha-amylase family derived from Aspergillus oryzae, was used as a model protein for high resolution X-ray crystal structure analysis. Space-grown crystals were obtained in the JAXA-GCF (Japan Aerospace Exploration Agency Granada Crystallization Facility) project [1]. Data collections was performed using synchrotron radiation from SPring-8 beamline BL44XU, equipped with a DIP6040 image plate detector (MAC Science / Bruker-AXS) at 90K under nitrogen vapour stream. Two data sets were collected for highand low-resolution data to obtain wide dynamic range diffraction data. The diffraction data were observed up to 0.94Å resolution. The data were integrated, scaled and merged using the DENZO and SCALEPACK programs. The crystals belong to space group P212121, with the following cell dimensions: a=50.4Å, b=67.4Å, c=130.5Å. The overall Rmerge based on intensities for all data was 7.7% with its completeness of 97.6%. The starting model for the refinement was the coordinate set 6TAA from the Protein Data Bank [2]. Refinement was carried out by SHELX-93. The last stage of refinement against data to 1.0Å converged to an R factor of 13.1% and a free R of 16.1%. The final model of taka-amylase consists of 4210 non-hydrogen atoms, 3148 hydrogen atoms and 671 water molecules. 13 side chains were modelled in two conformations. B factors were 11.7, 13.7 and 23.6Å for main-chain, side-chain and water molecules. This high-resolution structure was providing us more reliable geometric and conformational properties of the protein.

Trapping and mobility of soluble and insoluble impurities in ice monitoredviacryo-synchrotron-tomography