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. &nbsp;&nbsp;</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>