Crystallographic studies of biotechnology-relevant targets

Bioluminescence is a fascinating natural phenomenon where living organisms produce light through a biochemical reaction. Luciferases, the light-producing enzymes, typically sample huge protein conformational space, often preventing complete structural characterization by X-ray crystallography. Moreover, using a cognate substrate luciferin is problematic since its conversion into an oxyluciferin in the presence of the luciferase will prevent the capture of the enzyme-luciferin conformation in an activated state. In this experiment, we will demonstrate how to deal with such obstacles, focusing on the recent discoveries of marine bioluminescence mechanisms facilitated by a combination of engineered enzymes and the availability of a non-oxidizable luciferin analogue. Moreover, apolipoprotein E (ApoE) is a key player involved in neurodegeneration processes. In the proposed experiment, we aim to probe its interaction with dsDNA as well as with newly de novo designed protein binder.