Press Release / Health and Fitness / Crystal structures are still reveal novel features of protein folding & substrate binding in biosynthetic enzymes

Crystal structures are still reveal novel features of protein folding & substrate binding in biosynthetic enzymes

In a recent paper published in Nature Chemical Biology, new crystal structures provide insights into the evolution and activity of the AdoMet radical enzyme family that plays a critical role in purine biosynthesis. By crystallizing QueE in complex with its catalyst and substrates, they discovered that QueE contains a modified core fold unlike any other family member. A close look at the active site before and after substrate binding revealed even more secrets -- Read More.




These crystal structures were obtained using a codon-optimized QueE gene that was synthesized by GenScript.

GenScript has the expertise to rapidly synthesize codon-optimized gene constructs for the efficient expression of proteins you need for crystallography.

Don’t let molecular biology slow down your structural studies!