NMR experiments were acquired at 25 °C on Varian INOVA 600 and 750 MHz and Bruker Avance 900 MHz spectrometers equipped with cryogenic 1H{15N,13C} probes. The acquisition parameters for the experiments are provided in Table I . NMR spectra were processed using the program PROSA 6.4 and analyzed using the programs XEASY and CARA. 1H chemical shifts were referenced relative to internal DSS, and 13C and 15N chemical shifts were referenced indirectly via gyromagnetic ratios.
Avance 900 mhz
Manufactured by Bruker
The Avance 900 MHz is a high-field nuclear magnetic resonance (NMR) spectrometer developed by Bruker. It is designed to provide high-resolution NMR analysis capabilities for a wide range of applications in various scientific fields, including chemistry, materials science, and life sciences.
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4 protocols using avance 900 mhz
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NMR Experiments on Varian and Bruker Spectrometers
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NMR Spectroscopy of Calcium-Binding Proteins
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All NMR spectroscopy experiments were performed using a Bruker Avance 900 MHz spectrometers at Korean Basic Science Institute, Ochang. EfAcpA, EfAcpB and their mutants were dissolved in 25 mM MES buffer with 5mM CaCl2 at pH 6.1. For hydrogen/deuterium (H/D) exchange experiments, 15N-labeled samples at 0.5 mM were lyophilized, and 100% D2O was added immediately before performing NMR experiments. For 15 h, Heteronuclear single quantum coherence (HSQC) spectra were acquired every 10 min. The logP and ΔGlocal values of the residues were calculated as previously described [15 (link)].
3
Measuring Tau Protein 1JCaHa Couplings
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NMR samples contained 1 mM of 13 C/ 15 N-labeled Tau (the longest isoform with 441 residues) in 50 mM phosphate buffer, pH 6.0. NMR spectra were recorded at 278 K on a Bruker Avance 900 MHz spectrometer equipped with a cryogenic probe. For determination of 1 J CaHa couplings in Tau, a 3D (HA)CANH experiment was recorded, in which no decoupling was applied during the 13 C a evolution time. The 1 J CaHa coupling thus remained active during a 28 ms constant time evolution period, resulting in two highly resolved 13 C doublet components, which are split by the 1 J CaHa coupling (Zweckstetter and Bax 2001) . Taking into account the signal-to-noise ratio and the duration of the constant time evolution period (Kontaxis et al. 2000) (link), the experimental error in the 1 J CaHa couplings was estimated to be below 0.5 Hz. To avoid increased crowding relative to a regular (HA)CANH spectrum, the two doublet components were separated into two separate spectra by calculating the sum and difference of an in-phase and an anti-phase (HA)CANH spectrum (Zweckstetter and Bax 2001) .
Experimental 1 J CaHa couplings in a peptide comprising residues 201-219 of the splicing factor SRSF1 were previously measured using the same (HA)CANH experiment (Xiang et al. 2013; (link)Zweckstetter and Bax 2001) .
Experimental 1 J CaHa couplings in a peptide comprising residues 201-219 of the splicing factor SRSF1 were previously measured using the same (HA)CANH experiment (Xiang et al. 2013; (link)Zweckstetter and Bax 2001) .
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NMR Resonance Assignment of CaACP
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To assign the resonances of the backbone atoms and alpha protons of CaACP, we performed HNCO, HNCACB, CBCA(CO)NH, 2D 1 H-1 H nuclear Overhauser effect spectroscopy (NOESY), and total correlation spectroscopy (TOCSY) experiments using Bruker Avance 900 MHz spectrometers at KBSI (Ochang, Korea). All NMR spectra were processed with NMRPipe (Delaglio et al. 1995) (link) and analyzed using NMRFAM-Sparky (Lee et al. 2015) (link).
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