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Non‐Uniform Sampling and J‐UNIO Automation for Efficient Protein NMR Structure Determination
Author(s) -
Didenko Tatiana,
Proudfoot Andrew,
Dutta Samit Kumar,
Serrano Pedro,
Wüthrich Kurt
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201502544
Subject(s) - heteronuclear molecule , automation , nuclear magnetic resonance spectroscopy , two dimensional nuclear magnetic resonance spectroscopy , chemistry , heteronuclear single quantum coherence spectroscopy , residue (chemistry) , analytical chemistry (journal) , chromatography , stereochemistry , biochemistry , engineering , mechanical engineering
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.