Downloads
Application Note: Glycolytic Enzyme Enolase
The detailed understanding of three-dimensional protein structure is important in the design of new drugs and for engineering proteins with improved properties for industrial applications. X-ray diffraction is the most powerful method to determine the structure of such large molecules but can be applied only when suitable crystals are obtained. Unfortunately, not all proteins that are produced can crystallize readily and we need to identify the possible problems and try to fi nd a reasonable rationale for solving them.
Recombinant proteins with homogeneous quaternary structures crystallize with higher probability and give more reproducible results in biochemical assays than inhomogeneous recombinant proteins. Dynamic light scattering experiments allow us to identify substrate and analogs, which are amenable to crystallization. Ease of crystal growth and diffraction quality for a particular protein is highly consistent with the apparent monodispersity of the complex in solution, as judged by the DynaPro® dynamic light scattering.
The content you requested is only available to registered users of Bioresearch Online. By registering now, you'll get access to this piece of content and thousands of additional articles and product reviews across our entire network of sites.
