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Title: Crystal growth of phosphopantetheine adenylyltransferase, carboxypeptidase t, and thymidine phosphorylase on the international space station by the capillary counter-diffusion method

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.

Authors:
; ;  [1]; ;  [2];  [3]; ;  [1]
  1. Russian Academy of Sciences, Shubnikov Institute of Crystallography (Russian Federation)
  2. Russian Academy of Sciences, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry (Russian Federation)
  3. Research Institute for Genetics and Selection of Industrial Microorganisms, Scientific Center of Russian Federation (Russian Federation)
Publication Date:
OSTI Identifier:
22054256
Resource Type:
Journal Article
Journal Name:
Crystallography Reports
Additional Journal Information:
Journal Volume: 56; Journal Issue: 5; Other Information: Copyright (c) 2011 Pleiades Publishing, Ltd.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1063-7745
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CARBOXYPEPTIDASES; COMPLEXES; CRYSTAL GROWTH; CRYSTALS; DIFFUSION; ESCHERICHIA COLI; LIGANDS; MYCOBACTERIUM TUBERCULOSIS; PHOSPHOTRANSFERASES; SYNCHROTRON RADIATION; THERMOACTINOMYCES; THYMIDINE; TRANSFERASES; X-RAY DIFFRACTION

Citation Formats

Kuranova, I. P., E-mail: inna@ns.crys.ras.ru, Smirnova, E. A., Abramchik, Yu. A., Chupova, L. A., Esipov, R. S., Akparov, V. Kh., Timofeev, V. I., and Kovalchuk, M. V. Crystal growth of phosphopantetheine adenylyltransferase, carboxypeptidase t, and thymidine phosphorylase on the international space station by the capillary counter-diffusion method. United States: N. p., 2011. Web. doi:10.1134/S1063774511050154.
Kuranova, I. P., E-mail: inna@ns.crys.ras.ru, Smirnova, E. A., Abramchik, Yu. A., Chupova, L. A., Esipov, R. S., Akparov, V. Kh., Timofeev, V. I., & Kovalchuk, M. V. Crystal growth of phosphopantetheine adenylyltransferase, carboxypeptidase t, and thymidine phosphorylase on the international space station by the capillary counter-diffusion method. United States. doi:10.1134/S1063774511050154.
Kuranova, I. P., E-mail: inna@ns.crys.ras.ru, Smirnova, E. A., Abramchik, Yu. A., Chupova, L. A., Esipov, R. S., Akparov, V. Kh., Timofeev, V. I., and Kovalchuk, M. V. Thu . "Crystal growth of phosphopantetheine adenylyltransferase, carboxypeptidase t, and thymidine phosphorylase on the international space station by the capillary counter-diffusion method". United States. doi:10.1134/S1063774511050154.
@article{osti_22054256,
title = {Crystal growth of phosphopantetheine adenylyltransferase, carboxypeptidase t, and thymidine phosphorylase on the international space station by the capillary counter-diffusion method},
author = {Kuranova, I. P., E-mail: inna@ns.crys.ras.ru and Smirnova, E. A. and Abramchik, Yu. A. and Chupova, L. A. and Esipov, R. S. and Akparov, V. Kh. and Timofeev, V. I. and Kovalchuk, M. V.},
abstractNote = {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.},
doi = {10.1134/S1063774511050154},
journal = {Crystallography Reports},
issn = {1063-7745},
number = 5,
volume = 56,
place = {United States},
year = {2011},
month = {9}
}