Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution.

ABSTRACT: Structural genomics consortia established that protein crystallization is the primary obstacle to structure determination using x-ray crystallography. We previously demonstrated that crystallization propensity is systematically related to primary sequence, and we subsequently performed computational analyses showing that arginine is the most overrepresented amino acid in crystal-packing interfaces in the Protein Data Bank. Given the similar physicochemical characteristics of arginine and lysine, we hypothesized that multiple lysine-to-arginine (KR) substitutions should improve crystallization. To test this hypothesis, we developed software that ranks lysine sites in a target protein based on the redundancy-corrected KR substitution frequency in homologs. This software can be run interactiv

SUBMITTER: Banayan NE 

PROVIDER: S-EPMC10868448 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature