Crude butanol extracts were prepared from 7-day old agar cultures of S. ghanaensis ATCC 14672, S. hygroscopicus ATCC 53653, and WAC0256. The extracts were subjected to prefractionation and purification using an Alliance 2695 HPLC series (Waters). High-resolution ESI-MS was performed on Waters Micromass Quattro Ultima and Xevo G2-S Q-Tof mass spectrometers. One- and two-dimensional NMR data were acquired on a Bruker Avance III 700 MHz NMR spectrometer equipped with a 5 mm QNP cryoprobe, operating at 700.17 MHz for 1H NMR and 176.08 MHz for 13C NMR. The ACD Structure Elucidator software47 was used to elucidate the structure of dinactin.
5 mm qnp cryoprobe
Manufactured by Bruker
Sourced in Germany, United States, Canada
The 5 mm QNP cryoprobe is a specialized piece of laboratory equipment designed for nuclear magnetic resonance (NMR) spectroscopy. It is equipped with a quadruple-resonance (QNP) capability, allowing for the detection of multiple nuclei simultaneously. The cryogenic design of the probe helps maintain a low-temperature environment, improving signal-to-noise ratio and sensitivity during NMR experiments.
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Lab products found in correlation
Avance 3 700 mhz nmr spectrometer, by Bruker (3 mentions)
Avance 3 600 mhz instrument, by Bruker (2 mentions)
Xevo g2 s qtof, by Waters Corporation (1 mentions)
Micromass quattro ultima, by Waters Corporation (1 mentions)
Avance 500, by Bruker (1 mentions)
Acquity uplc xevo g2s qtof, by Waters Corporation (1 mentions)
Autopol 4, by Rudolph Research Analytical (1 mentions)
Du530 spectrophotometer, by Beckman Coulter (1 mentions)
Eclipse plus c18, by Agilent Technologies (1 mentions)
1290 hplc, by Agilent Technologies (1 mentions)
Inova 600 mhz spectrometer, by Agilent Technologies (1 mentions)
Q exactive orbitrap mass spectrometer, by Agilent Technologies (1 mentions)
Avance 3 700 mhz spectrometer, by Bruker (1 mentions)
Mnova nmr software, by Mestrelab Research (1 mentions)
7 protocols using 5 mm qnp cryoprobe
1
Structural Elucidation of Dinactin
2
NMR Data Acquisition Protocol
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Data was obtained on a Bruker Avance III 700 MHz NMR spectrometer (Bruker Biospin, Rheinstetten, Germany) equipped with a 5 mm QNP cryoprobe, operating at 700.17 MHz for 1H and controlled by TopSpin software (v.3.5 for Linux OS). Data was collected at room temperature, using a noesypr 1d pulse program with water suppression (Ravanbakhsh et al., 2015 (link)). The acquisition and mixing time were set to 4 s and 100 ms, respectively. Spectra was acquired with eight steady state scans with a field width of ≤80 Hz and O1P and spectral width were set to 4.69 and 12 ppm, respectively. Each sample was shimmed using a manual shimming protocol which included Z6 shimming along the Z-X-Y axes before the Z-X-Y-XZ-YZ axes to maintain a peak linewidth for DSS-d5 (<1 Hz) required for automated MAGMET spectral processing. Each sample required about 12 min to complete 128 scans.
3
NMR Spectroscopy of Platelet Metabolites
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Hydrophilic platelet metabolites were resuspended in a 600-µl D2O sodium phosphate buffer (0.1 M, pH 7.4) containing 0.25 mM 3-trimethylsilyl-2,2,3,3-d4-propionate (TSP) as an internal standard. NMR spectra were acquired from 500.13 MHz in Bruker Avance-500 spectrometers equipped with a 5-mm QNP CryoProbe (Bruker, BioSpin) at the Core Facility for Protein Structural Analysis supported by the National Core Facility Program for Biotechnology in Academia Sinica, Taiwan.
Both 1H and JRES NMR spectra were acquired at 300 K. 1H NMR spectra were acquired from the pulse sequence (relaxation delay: -90°-t-90°-tm-90°-acquired free induction decay) with presaturation of water resonance to suppress the water signal. For each sample, 32 k data points were collected from 128 scans in a 20-ppm spectral width with a 2.0-s relaxation delay and an acquisition time of 1.63 s. JRES NMR spectra were acquired from the pulse sequence (relaxation delay-90°-t1-180°-t1-acquired free induction delay, with water suppression during relaxation delay). Sixteen k data points in F2 frequency axis and 40 data points in F1 frequency axis were collected in eight scans with a 2.0-s relaxation delay. The spectral widths of the F2 and the F1 axis were set 6000 and 65 Hz, respectively.
Both 1H and JRES NMR spectra were acquired at 300 K. 1H NMR spectra were acquired from the pulse sequence (relaxation delay: -90°-t-90°-tm-90°-acquired free induction decay) with presaturation of water resonance to suppress the water signal. For each sample, 32 k data points were collected from 128 scans in a 20-ppm spectral width with a 2.0-s relaxation delay and an acquisition time of 1.63 s. JRES NMR spectra were acquired from the pulse sequence (relaxation delay-90°-t1-180°-t1-acquired free induction delay, with water suppression during relaxation delay). Sixteen k data points in F2 frequency axis and 40 data points in F1 frequency axis were collected in eight scans with a 2.0-s relaxation delay. The spectral widths of the F2 and the F1 axis were set 6000 and 65 Hz, respectively.
4
Analytical Characterization of Compounds
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High-resolution mass spectra were measured using an Acquity UPLC-Xevo G2-S QTof (Waters, Mississauga, Ontario, Canada). UV/visible spectra were recorded with a DU-530 Spectrophotometer (Beckman, Mississauga, Ontario, Canada). Optical rotation was measured on an Autopol IV automatic polarimeter (Rudolph Research Analytical, Hackettstown, NJ, USA). 1D and 2D NMR data were acquired on an Avance III 700 MHz NMR spectrometer (Bruker, Madison, WI, USA) equipped with a 5-mm QNP cryoprobe operating at 700.17 MHz for 1 H NMR and 176.08 MHz for 13 C NMR.
5
Spectroscopic Characterization of Molecules
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The NMR spectra were acquired on a Varian INOVA 600 MHz spectrometer (Mississauga, ON, Canada) equipped with a Varian 13 C enhanced HCN cold probe operating at 600.13 MHz for 1 H and 150.90 MHz for 13 C or a Bruker AVANCE III 700 MHz spectrometer (Milton, ON, Canada) equipped with a 5 mm QNP cryoprobe operating at 700.17 MHz for 1 H NMR and 176.08 MHz for 13 C NMR. All chemical shifts were referenced to the residual solvent peak for C 6 D 6 : 7.16 p.p.m. for 1 H and 128.5 p.p.m. for 13 C. Selective 1D 1 H NOE experiments used a 500 ms mixing time. NMR spectra were analyzed using Mnova NMR software (Mestrelab Research, ver. 10.0, Spain). HRESIMS data were acquired on a Thermo Q-Exactive Orbitrap mass spectrometer (Nepean, ON, Canada) with positive electrospray ionization (m/z range 100-1000), coupled to an Agilent 1290 HPLC (Mississauga, ON, Canada). For the chromatographic method, an Agilent EclipsePlusC18 (2.1 × 50 mm, 1.8 μm) column was used along with an 8 min gradient elution from 0 to 100% MeCN (+0.1% v/v formic acid) in H 2 O (+0.1% v/v formic acid) as the mobile phase. Specific rotation measurements were performed on a Rudolph Research Analytical Autopol IV automatic polarimeter (Mandel Scientific, Guelph, ON, Canada). Unless otherwise stated, all chemical reagents and microbiological media were purchased from Sigma-Aldrich (Oakville, ON, Canada).
6
NMR Spectroscopic Analysis of Organic Compounds
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Spectra were obtained using a Bruker Avance III 600 MHz instrument equipped with a Bruker QNP 5 mm cryoprobe (Bruker Biospin, Billerica, MA) at 30.0 ± 0.1 °C. NMR data is reported as follows: chemical shift (δ) (parts per million, ppm); multiplicity: m (multiplet), d (doublet), t (triplet), q (quartet), app t (apparent triplet), tt (triplet of triplets), qd (quartet of doublets), quin (quintet), sep (septet); coupling constants (J) are given in Hertz (Hz). 1H NMR (600 MHz) chemical shifts are calibrated with respect to residual DMSO-d5 in DMSO-d6 centered at 2.50 ppm, whereas for 13C NMR (151 MHz), the center peak for DMSO-d6, centered at 39.52 ppm, was used for the spectral calibration. For acquisitions in CDCl3, chemical shifts are calibrated with respect to residual chloroform in CDCl3 centered at 7.26 ppm, whereas for 13C NMR the center peak for CDCl3, centered at 77.0 ppm, was used for the spectral calibration. 13C-DEPT-135 NMR was used to identify the nature (i.e. 1°, 2°, 3° or quaternary) of the carbon atoms in the synthesized targets.
7
NMR Characterization of Organic Compounds
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Spectra were obtained using a Bruker Avance III 600 MHz instrument equipped with a Bruker QNP 5 mm cryoprobe (Bruker Biospin, Billerica, MA) at 30.0 ± 0.1°C. NMR data is reported as follows: chemical shift (δ) (parts per million, ppm); multiplicity: m (multiplet), d (doublet), t (triplet), q (quartet), app t (apparent triplet), tt (triplet of triplets), qd (quartet of doublets), sep (septet); coupling constants (J) are given in Hertz (Hz). 1H NMR (600 MHz) chemical shifts are calibrated with respect to residual HOD in D2O centered at 4.75 ppm. 13C-DEPT-135 NMR was used to identify the nature (i.e. 1o, 2o, 3o or quaternary) of the carbon atoms in the synthesized targets.
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