Use of massively multiple merged data for low-resolution S-SAD phasing and refinement of flavivirus NS1.

ABSTRACT: An emergent challenge in macromolecular crystallography is the identification of the substructure from native anomalous scatterers in crystals that diffract to low to moderate resolution. Increasing the multiplicity of data sets has been shown to make previously intractable phasing problems solvable and to increase the useful resolution in model refinement. For the West Nile virus nonstructural protein 1 (NS1), a protein of novel fold, the utility of exceptionally high multiplicity data is demonstrated both in solving the crystal structure from the anomalous scattering of the native S atoms and in extending the useful limits of resolution during refinement. A high-multiplicity data set from 18 crystals had sufficient anomalous signal to identify sulfur sites using data to 5.2 Å resolution.

SUBMITTER: Akey DL 

PROVIDER: S-EPMC4188011 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature