New scientific equipment for protein crystallization in microgravity, BELKA, and its approbation on the Bion-M No. 1 spa
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TAL GROWTH
New Scientific Equipment for Protein Crystallization in Microgravity, BELKA, and Its Approbation on the BionM No. 1 Spacecraft S. S. Baskakovaa, S. I. Kovalyova, V. A. Kramarenkoa, L. A. Zadorozhnayaa, M. S. Lyasnikovaa, Y. M. Dymshitsa, V. A. Shishkova, A. V. Egorovc, A. M. Dolginc, A. E. Voloshina, and M. V. Kovalchuka, b a
Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskii pr. 59, Moscow, 119333 Russia email: [email protected] b National Research Centre “Kurchatov Institute”, pl. Akademika Kurchatova 1, Moscow, 123182 Russia c Center for Operation of Space Ground Based Infrastructure, Moscow, Russia Received April 23, 2014
Abstract—A space experiment on the crystallization of lisozyme and glucose isomerase proteins in UK1 and UK2 crystallizers on the scientific equipment BELKA on the BionM no. 1 spacecraft was performed in April–May 2013. A groundbased experiment was carried out simultaneously at the Institute of Crystallog raphy of the Russian Academy of Sciences (IC RAS). Transparent crystals were obtained in both cases. The lisozyme crystals grown in microgravity are larger than their terrestrial analogs. An optical study of glucose isomerase crystals grown in space has shown that the coalescence of equally oriented crystallites leads to the formation of quasisinglecrystal blocks. An Xray diffraction experiment on lisozyme crystals has revealed the resolutions for crystals obtained under terrestrial conditions and in space to be 1.74 and 1.58 Å, respec tively. DOI: 10.1134/S1063774515010046
INTRODUCTION Currently, the main method for studying the struc ture of protein molecules with atomic resolution is the Xray diffraction analysis of single crystals of a given material [1]. The error in solving the atomic structure depends directly on the structural quality of the single crystals used. The results of numerous experiments indicate that protein crystals grown in space have a higher structural quality. Convective flows are almost completely suppressed in microgravity, and mass transfer in solution is mainly due to diffusion [2]. An impurity that can block kinks and reduce the growth rate has a lower diffusion rate and a higher distribution coefficient than protein mol ecules. Under these conditions, the impurity concen tration at the crystal–solution interface is lower, and crystal grows in an impuritydepleted field. The first space experiment (SE) was performed in 1981 on a German TEXUS rocket. Crystals of β galactosidase and lisozyme were grown by diffusion in liquid. The crystallizer consisted of three reservoirs which were separated by a mobile partition and con tained buffer, protein, and salt solutions. Displace ment of the participation facilitated contact of solu tions and diffusion of macromolecules and ions through the buffer layer. It was rather difficult to
choose appropriate crystallization conditions on earth because of the different densities of the solutions [3]. In 1983 the European Space Agency, in collabora tion with the N
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