Crystallization and structure determination of delta-subunit of RNApolymerase

• 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
• 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.

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