A new soaking procedure for X-ray crystallographic structural determination of protein-peptide complexes.

ABSTRACT: Interactions between a protein and a peptide motif of its protein partner are prevalent in nature. Often, a protein also has multiple interaction partners. X-ray protein crystallography is commonly used to examine these interactions in terms of bond distances and angles as well as to describe hotspots within protein complexes. However, the crystallization process presents a significant bottleneck in structure determination since it often requires notably time-consuming screening procedures, which involve testing a broad range of crystallization conditions via a trial-and-error approach. This difficulty is also increased as each protein-peptide complex does not necessarily crystallize under the same conditions. Here, a new co-crystallization/peptide-soaking method is presented which circumv

SUBMITTER: Ballone A 

PROVIDER: S-EPMC7531243 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature