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4 results for “HTT domain”
Coexpression and purification of HTT domains with HAP40 - 2018/12/03
<p><strong>Project: </strong>High resolution structural analysis of purified HTT proteins</p> <p><strong>Experiment: </strong>Coexpression and purification of HTT domains with HAP40</p> <p><strong>Date completed:­ </strong>2018/12/03</p> <p><strong>Rationale: </strong>HTT domain fragments are challenging to express and purify. However, the full-length protein sample was shown to have superior biophysical characteristics when coexpressed and purified with HAP40. As HAP40 has an extensive interaction surface with HTT, it could be possible to copurify domain fragments of HTT with HAP40, stabilizing the individual HEAT domains. </p>
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>
Purification of the HTT C-HEAT domain (2088-3144)
<p>The purification of HTT fragments is a useful approach to learn more about the function of huntingtin in the cell. By obtaining soluble and monomeric samples of HTT domains namely the HTT C-HEAT, N-HEAT and bridge domains, specific protein-protein interactions can be studied. Furthermore, domains of HTT in soluble monomeric form could enable crystallization studies. </p> <p>Expression and purification of these fragments can be found on these posts <a href="https://zenodo.org/record/2600051#.XKU89aeZPOQ">https://zenodo.org/record/2600051#.XKU89aeZPOQ</a> and <a href="https://zenodo.org/record/2628060#.XULMtnspDb0">https://zenodo.org/record/2628060#.XULMtnspDb0</a> (performed by Dr. Rachel Harding). The latest post shows the successful purification of a monomeric and mono disperse sample of the HTT C-HEAT domain. The results here presented are a follow up of those experiments and aim to further characterize the HTT C-HEAT domain as well as explore strategies to improve buffer conditions for crystallization purposes.</p>
DLS on HTT C-HEAT and N-HEAT domains
<p>Raw data and summary of results of DLS data recorded for C-HEAT_2088-3144 (TOC019 C01), and constructs of the N-HEAT domain: N-HEAT_76-404 (TOC019 B02), N-HEAT_ 93-404 (TOC019 A03), <a href="https://zenodo.org/record/3462496#.XY4U1mYpA2x">N-HEAT_81-1643 (TOC019 B08)</a>, N-HEAT_76-1715 (TOC019 A08).</p>
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