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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2011-09

AUTHORS

I. P. Kuranova, E. A. Smirnova, Yu. A. Abramchik, L. A. Chupova, R. S. Esipov, V. Kh. Akparov, V. I. Timofeev, M. V. Kovalchuk

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. More... »

PAGES

884

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s1063774511050154

DOI

http://dx.doi.org/10.1134/s1063774511050154

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1039322772


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