Abstract
Crystals of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis, thymidine phosphorylase from Escherichia coli, carboxypeptidase T from Thermoactinomyces vulgaris and its mutant forms, and crystals of complexes of these proteins with functional ligands and inhibitors were grown by the capillary counter-diffusion method in the Japanese Experimental Module Kibo on the International Space Station. The high-resolution X-ray diffraction data sets suitable for the determination of high-resolution three-dimensional structures of these proteins were collected from the grown crystals on the SPring-8 synchrotron radiation facility. The conditions of crystal growth for the proteins and the data-collection statistics are reported. The crystals grown in microgravity diffracted to a higher resolution than crystals of the same proteins grown on Earth.
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Original Russian Text © I.P. Kuranova, E.A. Smirnova, Yu.A. Abramchik, L.A. Chupova, R.S. Esipov, V.Kh. Akparov, V.I. Timofeev, M.V. Kovalchuk, 2011, published in Kristallografiya, 2011, Vol. 56, No. 5, pp. 944–951.
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Kuranova, I.P., Smirnova, E.A., Abramchik, Y.A. et al. Crystal growth of phosphopantetheine adenylyltransferase, carboxypeptidase t, and thymidine phosphorylase on the international space station by the capillary counter-diffusion method. Crystallogr. Rep. 56, 884–891 (2011). https://doi.org/10.1134/S1063774511050154
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DOI: https://doi.org/10.1134/S1063774511050154