Many proteins do not crystallize on their own, restricting our capacity to determine their structure using techniques such as x-ray crystallography. Chaperone proteins show potential to mitigate this problem by binding to and forcing these recalcitrant proteins into crystals. However, because some of these crystals do not diffract well, it is hypothesized that an overly long or flexible linker between TELSAM and the target protein may allow for too much movement in the crystal lattice. To determine if shortening and rigidifying the linker can solve the problem and yield well-diffracting crystals, chaperone-target constructs were engineered with different linkers using 1TEL constructs with the target proteins CMG2, UBA, and DARPin with variations in linker lengths and flexibility. After purifying and crystallizing the proteins, x-ray diffraction data are collected and the structures solved using Phenix, Coot, and Pymol software. The new TELSAM complexes yielded well-diffracting crystals, indicating that these shorter and more rigid linkers may effectively mitigate the poor resolution issues of TELSAM-target construct crystals.

Shortening and rigidifying the TELSAM-target protein linker for improved crystal diffraction quality

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