Large-scale purification of HTT domain constructs 2019/04/01

doi:10.5281/zenodo.2628060

Published April 1, 2019 | Version v1

Dataset Open

Large-scale purification of HTT domain constructs 2019/04/01

1. Structural Genomics Consortium, University of Toronto
2. Structural Genomics Consortium, University of Toronto, MaRS South Tower, 101 College Street, Toronto, Ontario M5G 1L7, Canada
3. CHDI Foundation

Project: High resolution structural analysis of purified HTT samples

Experiment: Large-scale purification of HTT domain constructs

Date completed: 2019/04/01

Rationale: Domain fragments of the huntingtin protein are useful reagents for examining protein-protein interaction characteristics of huntingtin and to map interaction interfaces. Stable, monodisperse and pure samples may also be amenable to high resolution structure solution by X-ray crystallography. Previously huntingtin fragments were cloned and screened for expression in small-scale (3 mL) culture experiments. Positive hits were scaled for production as detailed in the table on the next page. All previous work is described in this post:https://zenodo.org/record/2600051#.XKU89aeZPOQ.

Notes

Dr. Harding is the recipient of the Huntington's Disease Society of America Berman Topper Career Development Fellowship which funds and supports this research, in addition to generous funding from the CHDI Foundation and the Huntington Society of Canada. The SGC is a registered charity (number 1097737) that receives funds from AbbVie, Bayer Pharma AG, Boehringer Ingelheim, Canada Foundation for Innovation, Eshelman Institute for Innovation, Genome Canada through Ontario Genomics Institute [OGI-055], Innovative Medicines Initiative (EU/EFPIA) [ULTRA-DD grant no. 115766], Janssen, Merck KGaA, Darmstadt, Germany, MSD, Novartis Pharma AG, Ontario Ministry of Research, Innovation and Science (MRIS), Pfizer, São Paulo Research Foundation-FAPESP, Takeda, and Wellcome.

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