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1.
Figure 3

Figure 3. From: In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.

2D 13C-13C PARIS spectra of 13C, 15N uniformly enriched LR11 TM in native E. coli membranes recorded for resonance assignment with (a) 5 ms mixing time and 96 scans per t1 point; (b) 20 ms mixing time and 112 scans per t1 point; (c) 100 ms mixing time and 128 scans per t1 point. The acquisition times for direct and indirect dimensions were 10.3 and 4.8 ms, and the recycle delay was 1.5 s.

Riqiang Fu, et al. J Am Chem Soc. ;133(32):12370-12373.
2.
Figure 1

Figure 1. From: In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.

(a) Primary structure of the LBT-LR11TM-His6. The LR11 fragment is shown in bold, corresponding to residues 2132 to 2161 of the full-length protein. The LBT (lanthanide binding tag) is shown in italics. (b) SDS-PAGE results for the preparation of LR11 TM in native E. coli membranes. Lanes: 1, protein marker; 2, isolated E. coli membrane fraction; 3, thrombin cleavage of the sample in lane 2; 4, buffer washes of the sample in lane 3; 5, prepared membrane fraction for NMR experiments.

Riqiang Fu, et al. J Am Chem Soc. ;133(32):12370-12373.
3.
Figure 2

Figure 2. From: In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.

13C MAS spectra of 13Cα,β-Ala enriched LR11 TM in native E. coli membranes recorded at 305 K on a Bruker 600 MHz spectrometer using a home-built low-E 3.2 mm probe. The spinning rate was 10 kHz. (a) 1D spectra recorded using DP, CP and CP-DQF polarization schemes with 512, 512 and 2048 scans, 5, 2 and 2s recycle delays, respectively. (b) A 2D 13C-13C PARIS spectrum collected with 20 ms mixing time, 9.2 and 7.0 ms acquisition time for direct and indirect dimensions, 1.5 s recycle delay and 512 scans per t1 point.

Riqiang Fu, et al. J Am Chem Soc. ;133(32):12370-12373.

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