Engineered antigen-binding fragments for enhanced crystallization of antibody:antigen complexes.

ABSTRACT: The atomic-resolution structural information that X-ray crystallography can provide on the binding interface between a Fab and its cognate antigen is highly valuable for understanding the mechanism of interaction. However, many Fab:antigen complexes are recalcitrant to crystallization, making the endeavor a considerable effort with no guarantee of success. Consequently, there have been significant steps taken to increase the likelihood of Fab:antigen complex crystallization by altering the Fab framework. In this investigation, we applied the surface entropy reduction strategy coupled with phage-display technology to identify a set of surface substitutions that improve the propensity of a human Fab framework to crystallize. In addition, we showed that combining these surface substitutions w

SUBMITTER: Bruce HA 

PROVIDER: S-EPMC10731619 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature