Extending the scope of coiled-coil crystal structure solution by AMPLE through improved ab initio modelling.

ABSTRACT: The phase problem remains a major barrier to overcome in protein structure solution by X-ray crystallography. In recent years, new molecular-replacement approaches using ab initio models and ideal secondary-structure components have greatly contributed to the solution of novel structures in the absence of clear homologues in the PDB or experimental phasing information. This has been particularly successful for highly α-helical structures, and especially coiled-coils, in which the relatively rigid α-helices provide very useful molecular-replacement fragments. This has been seen within the program AMPLE, which uses clustered and truncated ensembles of numerous ab initio models in structure solution, and is already accomplished for α-helical and coiled-coil structures. Here, an expansion in t

SUBMITTER: Thomas JMH 

PROVIDER: S-EPMC7057219 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature