LAUSR

Cryo-EM has recently been recognized as a major tool for obtaining protein structures at near-atomic resolution. The use of this technique has skyrocketed in recent years, due to certain technological advancements. This includes not only direct detectors and phase plates, but also software tools such as Relion [1], cryoSparc [2], and Coot [3]. At this stage, biochemical protein purification remains a bottleneck. This step is difficult to automate because it relies substantially on human expertise. A number of problems associated with the difficulties of choosing a protein expression system, method of purification, and concentration of functional protein remain. The overall goal is to minimize the number of purification steps, to minimize the impact of purification procedures on the object and to obtain a suitable amount of pure sample in a native environment.