Large-scale purification of HTT domain constructs 2019/04/01
<p><strong>Project: </strong>High resolution structural analysis of purified HTT samples</p> <p><strong>Experiment: </strong>Large-scale purification of HTT domain constructs</p> <p><strong>Date completed:­ </strong>2019/04/01</p> <p><strong>Rationale: </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. 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:<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
Topics
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