Abstract by Neal Munson
Chemistry and Biochemistry
Giving Crystallization its Scaffolds
The crystallization of proteins serves as an effective way to find their structure by X-ray diffraction. However, forming a consistent protein lattice is a challenge, and thus only a portion of the millions known have been imaged with X-ray diffraction. For this reason, we investigate the technique of using a generic scaffold protein that readily crystallizes to pull linked proteins into a crystalline lattice. We engineer commonly used proteins such as GFP, lysozyme, and Maltose Binding Protein to form ordered symmetrical polymers. Those that yield the best diffracting crystals will be linked to proteins not yet crystallized such as the radical SAM protein GD-AE, aRNR-AE, and complexes of HydE, HydF, and HydG. Applying this technique, we can increase protein crystallization success rate. This will expedite the process to study an unknown or designed protein’s structure and function.