We've updated our Privacy Policy to make it clearer how we use your personal data. We use cookies to provide you with a better experience. You can read our Cookie Policy here.

Advertisement

How Size Exclusion Chromatography Illuminates Protein Crystallization

Listen with
Speechify
0:00
Register for free to listen to this article
Thank you. Listen to this article using the player above.

Want to listen to this article for FREE?

Complete the form below to unlock access to ALL audio articles.

Read time: Less than a minute

‘Analysis of membrane protein by multi-detector SEC’ describes how the Viscotek TDAmax size exclusion chromatography (SEC) system was used to characterize and optimize the proportion of protein and detergent in a purified membrane protein sample.

Crystallization of a membrane protein can depend on many factors, such as protein purity and the detergent concentration or type. Removing too much of the detergent component of a membrane protein complex can lead to degradation of the protein and reduce the chances of crystallization.

In this application note, the protein detergent complex (PDC), a bacterial membrane protein involved in multidrug resistance, is characterized using the Viscotek TDAmax system, a complete size-exclusion chromatography system with refractive index (RI), ultraviolet (UV), light scattering (LS) and intrinsic viscosity (IV) detectors. The molecular weight of the PDC and of the free detergent n-dodecyl β-D-maltoside (DDM) micelles was measured. Furthermore, the composition of the PDC, in terms of protein and DDM content, was measured and found to be very close to expectations.

Analysis of membrane protein by multi-detector SEC is available here