期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 7, 期 14, 页码 2821-2825出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.6b01074
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资金
- Agence Nationale pour la Recherche [ANR-14-ACHN-0015-01]
- Fondation Claude et Giuliana, Vaduz, Liechtenstein
- ERC [647474]
- European Research Council (ERC) [647474] Funding Source: European Research Council (ERC)
- Agence Nationale de la Recherche (ANR) [ANR-14-ACHN-0015] Funding Source: Agence Nationale de la Recherche (ANR)
In-cell NMR spectroscopy provides atomic resolution insights into the structural properties of proteins in cells, but it is rarely used to solve entire protein structures de novo. Here, we introduce a paramagnetic lanthanide-tag to simultaneously measure protein pseudocontact shifts (PCSs) and residual dipolar couplings (RDCs) to be used as input for structure calculation routines within the Rosetta program. We employ this approach to determine the structure of the protein G B1 domain (GB1) in intact Xenopus laevis oocytes from a single set of 2D in-cell NMR experiments. Specifically, we derive well-defined GB1 ensembles from low concentration in-cell NMR samples (similar to 50 mu M) measured at moderate magnetic field strengths (600 MHz), thus offering an easily accessible alternative for determining intracellular protein structures.
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