2012
DOI: 10.1038/nmeth.2248
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Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals

Abstract: Membrane proteins are largely underrepresented among available atomic-resolution structures. The use of detergents in protein purification procedures hinders the formation of well-ordered crystals for X-ray crystallography and leads to slower molecular tumbling, impeding the application of solution-state NMR. Solid-state magic-angle spinning NMR spectroscopy is an emerging method for membrane-protein structural biology that can overcome these technical problems. Here we present the solid-state NMR structure of… Show more

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Cited by 149 publications
(168 citation statements)
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“…Chemical shifts were calibrated using DSS as internal reference [3] . Spinal-64 [4] was applied for high power 1 H- 13 C decoupling (amplitude of 83 kHz) during evolution and detection periods. A ramped cross-polarization with contact time of 1.2-1.75 ms was used for the initial 1 H- 13 C and 1 H-15 N transfers.…”
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confidence: 99%
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“…Chemical shifts were calibrated using DSS as internal reference [3] . Spinal-64 [4] was applied for high power 1 H- 13 C decoupling (amplitude of 83 kHz) during evolution and detection periods. A ramped cross-polarization with contact time of 1.2-1.75 ms was used for the initial 1 H- 13 C and 1 H-15 N transfers.…”
mentioning
confidence: 99%
“…Spinal-64 [4] was applied for high power 1 H- 13 C decoupling (amplitude of 83 kHz) during evolution and detection periods. A ramped cross-polarization with contact time of 1.2-1.75 ms was used for the initial 1 H- 13 C and 1 H-15 N transfers.  U-13 C, 15 N-FimA sample in 4 mm rotor at 850 MHz: 2D 13 C- 13 C experiments were recorded using a PDSD mixing period of 50 ms (exp.…”
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confidence: 99%
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