ARCIMBOLDO at low resolution: Verification for coiled coils and globular proteins.

ABSTRACT: Crystallography at low resolution must determine the atomic model from less experimental observations, which is challenging in the absence of a model. In addition, model bias is more severe when independent experimental data are scarce. Our methods solve the phase problem by combining the location of accurate model fragments using Phaser with density modification and interpretation of the resulting maps using SHELXE. From a partial, correct structure, the density modification process and the stereochemical constraints draw the rest of the structure, validating the result. This same principle is now exploited at low resolution. Coiled coils are important, ubiquitous structures but notoriously difficult to phase and to predict. Both correct solutions and incorrect ones are poorly discriminat

SUBMITTER: Caballero I 

PROVIDER: S-EPMC11328115 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature