Research data supporting "Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis"
Brown, Steven P.
University of Cambridge
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Nikolovski, N., Dupree, R., Brown, S. P., & Dupree, P. (2016). Research data supporting "Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis" [Dataset]. https://doi.org/10.17863/CAM.68993
1D solid state NMR data for mature stems of stello cellulose synthesis mutant and wild type plants. MAS solid state NMR experiments were performed on a widebore Bruker (Karlsruhe, Germany) AVANCE III 850 MHz solid state NMR spectrometer operating at 20 T, corresponding to 1H and 13C Larmor frequencies of 850.2 and 213.8 MHz, respectively, using a 4 mm double-resonance MAS probe. Experiments were conducted at room temperature at a MAS frequency of 12.0 kHz ± 5 Hz. The 13C cross-polarization (CP) MAS spectra were acquired using a 1ms ramped contact time, a spectral window of 100 kHz (468 ppm), a recycle delay of 2 s and 28800 transients were co-added for each sample. The 1H 90° pulse duration was 3.4 s. Two-pulse phase-modulated (TPPM) decoupling was applied during acquisition at a 1H nutation frequency of 83 kHz58. The 13C chemical shift was determined using the carbonyl peak at 177.8 ppm of L-alanine as an external reference with respect to TMS. Two independent stem samples were analysed.
This research data supports “Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis” which will be published in “Nature communications”.
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stello, solid state NMR, arabidopsis
Publication Reference: https://doi.org/10.1038/ncomms11656
This work was supported by the BBSRC [grant number BB/G016240/1].
This record's DOI: https://doi.org/10.17863/CAM.68993
Attribution 2.0 UK: England & Wales
Licence URL: http://creativecommons.org/licenses/by/2.0/uk/
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