Crystallization and structure determination of delta-subunit of RNApolymerase

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Authors	DEMO Gabriel PAPOUŠKOVÁ Veronika ŠANDEROVÁ Hana ŽÍDEK Lukáš WIMMEROVÁ Michaela
Year of publication	2011
Type	Conference abstract
MU Faculty or unit	Central European Institute of Technology
Citation
Description	The structure of N-terminal domain was determined by NMR. It consists mainly of three alpha-helixes and one short beta-sheet, yet the N-terminal part remains unstructured. The cause of this flexibility is probably the His6-Tag attached at the N-terminus.The N-terminal domain of delta subunit was conquested to high-throughput screening (sitting drop), where several crystallization conditions were found.Higher quality crystals were obtained after 7-9 days with an average size 150 x 100 micrometers.Diffraction data were collected at ESRF Grenoble, ID-23. The resolution of the structure was 3.5 Angstrom. The data were processed by MOSFLM and the determination of the structure was done by molecular replacement with NMR structure used as a model.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Molekulární a strukturní biologie vybraných cytostatik. Od mechanických studií k chemoterapii rakoviny Delta podjednotka RNA polymerázy z Gram pozitivních bakterií