Protein crystallization under microgravity conditions. Analysis of the results of Russian experiments performed on the I
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Protein Crystallization under Microgravity Conditions. Analysis of the Results of Russian Experiments Performed on the International Space Station in 2005−2015 K. M. Boykoa,b,*, V. I. Timofeeva,c, V. R. Samyginaa,c, I. P. Kuranovaa,c, V. O. Popova,b, and M. V. Koval’chuka,c aNational
Research Centre “Kurchatov Institute”, pl. Akademika Kurchatova 1, Moscow, 123098 Russia Federal Research Centre “Fundamentals of Biotechnology”, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 119071 Russia c Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, Leninskii pr. 59, Moscow, 119333 Russia *e-mail: [email protected] b
Received May 6, 2016
Abstract—Conditions of mass transport to growing crystals have a considerable effect on the crystal size and quality. The reduction of convective transport can help improve the quality of crystals for X-ray crystallography. One approach to minimizing convective transport is crystallization in a microgravity environment, in particular, in space. The data obtained by our research team in protein crystallization experiments on the International Space Station are surveyed and analyzed. DOI: 10.1134/S1063774516050059
CONTENTS Introduction 1. Russian Experiments on Protein Crystal Growth under Microgravity Conditions 1.1. Module 1 1.2. JAXA Crystallization Box 2. The Most Remarkable Results Obtained in the Framework of Russian−Japanese Experiments Conclusions INTRODUCTION Structural biology is one of the most important branches of modern physicochemical biology. Knowledge of the three-dimensional structures of biological macromolecules (proteins and nucleic acids) is of great importance for understanding molecular mechanisms of the action of cells and their components [1]. The determination of the three-dimensional structure of the target protein is essential for the search for new promising molecules that can serve as the basis for drugs [2, 3], as well as for the design and optimization of new biocatalysts for different fields of biotechnology [4]. X-ray crystallography is currently the most favored technique for investigating the three-dimensional structures of macromolecules. As of April 2016, there
are more than 117 000 different structures in the Protein Data Base (www.rcsb.org), almost 90% of which were determined by this technique. The main limitation of X-ray crystallography is that it involves the crystallization of samples as a preliminary step, which often constitutes a bottleneck [5, 6]. The quality of grown crystals is responsible for the resolution of X-ray diffraction data and, finally, for the accuracy and precision of structural information. The general principle of crystallization of macromolecules from solution is to reduce their solubility until the supersaturation is reached by varying such parameters as pH, temperature, precipitant concentration, etc. [6, 7]. During crystal growth, the mass transport to the growing crystal occurs through two mechanisms─diffusion and convection
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