Work

Non‐Uniform Sampling and J‐UNIO Automation for Efficient Protein NMR Structure Determination

Year: 2015

Type: article

Abstract: High-resolution structure determination of small proteins in solution is one of the big assets of NMR spectroscopy in structural biology. Improvements in the efficiency of NMR structure determination by advances in NMR experiments and automation of data handling therefore attracts continued interest. Here, non-uniform sampling (NUS) of 3D heteronuclear-resolved [(1)H,(1)H]-NOESY data yielded two- to three-fold savings of instrument time for structure determinations of soluble proteins. With the 152-residue protein NP_372339.1 from Staphylococcus aureus and the 71-residue protein NP_346341.1 from Streptococcus pneumonia we show that high-quality structures can be obtained with NUS NMR data, which are equally well amenable to robust automated analysis as the corresponding uniformly sampled data.

Source: Chemistry - A European Journal

DOI: 10.1002/chem.201502544

Authors: Tatiana Didenko, Andrew Proudfoot, Samit Kumar Dutta, Pedro Serrano, Kurt Wüthrich

Institutions: Scripps Research Institute, Joint Center for Structural Genomics

Language: English

Topic: Advanced NMR Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institute of General Medical Sciences, Common Fund

Awards: Joint Center for Structural Genomics (JCSG-2), JCIMPT-Complexes, GPCR Network, G7967368859, G846886665