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

<p><strong>Project:&nbsp;</strong>High resolution structural analysis of purified HTT samples</p> <p><strong>Experiment:&nbsp;</strong>Large-scale purification of HTT domain constructs</p> <p><strong>Date completed:&shy;&nbsp;</strong>2019/04/01</p> <p><strong>Rationale:&nbsp;</strong>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.&nbsp;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.&nbsp;&nbsp;&nbsp;All previous work is described in this post:<a href="https://zenodo.org/record/2600051#.XKU89aeZPOQ">https://zenodo.org/record/2600051#.XKU89aeZPOQ</a>.</p>

ShareScore

36/100

Overall dataset sharing score

Score breakdown

These five areas show where the dataset supports — or may limit — practical reuse.

Stewardship
8
Harmonization
4
Access
16
Reuse readiness
8
Engagement
0

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