Gabrielsen, M. , Kroner, F., Black, I., Isaacs, N.W., Roe, A.J. and McLuskey, K. (2011) High-throughput identification of purification conditions leads to preliminary crystallization conditions for three inner membrane proteins. Molecular Membrane Biology, 28(7-8), pp. 445-453. (doi: 10.3109/09687688.2011.628954) (PMID:22034843)
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Abstract
An important factor in the crystallization, and subsequent structural determination, of integral membrane proteins is the ability to produce a stable and monodisperse solution of the protein. Obtaining the correct purification detergent to achieve this can be laborious and is often serendipitous. In this study, high-throughput methods are used to analyze the suitability of eight different detergents on the stability of 12 inner transmembrane proteins from <i>Escherichia coli</i>. The best results obtained from the small-scale experiments were scaled up, the aggregation state of the proteins assessed, and all monodisperse protein solutions entered into crystallization trials. This resulted in preliminary crystallization hits for three inner membrane proteins: XylH, PgpB and YjdL and this study reports the methods, purification procedures and crystallization conditions used to achieve this.
| Item Type: | Articles |
|---|---|
| Keywords: | High-throughput, inner transmembrane protein, detergents, crystallization |
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Black, Mrs Isobel and Gabrielsen, Dr Mads and McLuskey, Dr Karen and Roe, Professor Andrew and Isaacs, Professor Neil |
| Authors: | Gabrielsen, M., Kroner, F., Black, I., Isaacs, N.W., Roe, A.J., and McLuskey, K. |
| Subjects: | Q Science > QH Natural history > QH345 Biochemistry |
| College/School: | College of Medical Veterinary and Life Sciences > School of Infection & Immunity College of Science and Engineering > School of Chemistry |
| Journal Name: | Molecular Membrane Biology |
| Publisher: | Informa Healthcare |
| ISSN: | 0968-7688 |
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