800 mhz spectrometer

Manufactured by Bruker

Sourced in Germany, United States

The 800 MHz spectrometer is a high-performance nuclear magnetic resonance (NMR) instrument designed for advanced structural and analytical applications. It features a superconducting magnet that generates a strong magnetic field, enabling the acquisition of high-resolution NMR data. The spectrometer is capable of performing a variety of NMR experiments, providing users with detailed information about the chemical and structural properties of the samples under investigation.

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Lab products found in correlation

Topspin 3, by Bruker (7 mentions) Cryoprobe, by Bruker (3 mentions) 500 mhz spectrometer, by Bruker (3 mentions) Triple resonance cryoprobe, by Bruker (2 mentions) Txo cryogenic probe, by Bruker (2 mentions) 700 mhz spectrometer, by Agilent Technologies (2 mentions) Topspin v3, by Bruker (2 mentions) Tci cryoprobe, by Bruker (1 mentions) Topspin, by Bruker (1 mentions) 3.2 mm triple resonance mas probe, by Bruker (1 mentions) Avance 600 mhz spectrometer, by Bruker (1 mentions) Molmol, by Schrödinger (1 mentions) Chelex 100, by Bio-Rad (1 mentions) Inova 600 mhz spectrometer, by Agilent Technologies (1 mentions) 900 mhz spectrometer, by Bruker (1 mentions) Yeast trna, by Thermo Fisher Scientific (1 mentions) Spectramax i3x, by Molecular Devices (1 mentions) Txi probe, by Bruker (1 mentions) Bms 005b, by Wilmad (1 mentions) Triple resonance hcn cryo probe, by Bruker (1 mentions)

Spelling variants of this product

Bruker spectrometers (71 citations) Avance III 800 MHz NMR spectrometer (6 citations) DRX 800 MHz spectrometer (6 citations) SPE-800 MHz NMR-MS Spectrometer (5 citations) (800 or 900 MHz) spectrometers (4 citations) AVIII 800 MHz spectrometer (3 citations) Avance 800 MHz NMR spectrometer (3 citations) AVANCE NEO 800 MHz spectrometer (3 citations) 800- or 900-MHz NMR spectrometer (2 citations) AVANCE HD 800 MHz NMR spectrometer (2 citations)

79 protocols using 800 mhz spectrometer

NMR Characterization of VDAC-1 in Nanodiscs

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[U-²H,¹⁵N] labeled VDAC-1 in DMPC:DMPG (3:1) nanodiscs (611 µM and 500 µM of VDAC1 in cNW9 and cNW11 nanodiscs, respectively) were prepared as described above in NMR buffer (20 mM NaPO₄, 50 mM NaCl, 5 mM DTT, 1 mM EDTA, pH 7.0, 6% D₂O). ¹⁵N-TROSY HSQC data were collected at 45°C on a Bruker 800-MHz spectrometer equipped with a TXO cryogenic probe. Data for VDAC-1 in cNW9 and cNW11 nanodiscs were acquired with 48 and 96 scans, respectively, and 128 complex points in the ¹⁵N-indrect dimension.
The ¹⁵N-TROSY HSQC spectrum of 40 µM ¹⁵N-labeled NTR1 in cNW9 nanodiscs was acquired at 45°C on a Bruker 800-MHz spectrometer. Data were collected with 2048 scans per FID and 36 non-uniformly sampled ¹⁵N-dimension complex points (maximum point of 64). The ¹⁵N-dimension time domain data were reconstructed with hmsIST²⁶ and processed by NMRPipe software programs²⁷.

Nasr M.L., Baptista D., Strauss M., Sun Z.Y., Grigoriu S., Huser S., Plückthun A., Hagn F., Walz T., Hogle J.M, & Wagner G. (2016). Covalently circularized nanodiscs for studying membrane proteins and viral entry. Nature methods, 14(1), 49-52.

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NMR Backbone Assignment of h-Galectin-4 CRD

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The backbone resonance assignment of the N-terminal CRD of hGalectin-4 was performed at 25°C on an 800 MHz Bruker spectrometer equipped with a cryoprobe (Bruker, Billerica, MA, United States). 3D HNCO, HN(CA)CO, HN(CO)CACB, and HNCACB experiments were performed and assigned for the free Gal-4N containing the His-Tag and for Gal-4N without the His-Tag in the presence of 200 equivalents of lactose. Additionally, HN(CO)CA and HNCA experiments were recorded for the free protein containing the His-Tag. The entire analysis provided the unambiguous identification of 80% of the expected NH signals for Gal-4N. The spectra were processed with Bruker TopSpin 3.5.2 (Bruker, Billerica, MA, United States) and analyzed via CARA NMR 1.9.1.4.

Quintana J.I., Delgado S., Núñez-Franco R., Cañada F.J., Jiménez-Osés G., Jiménez-Barbero J, & Ardá A. (2021). Galectin-4 N-Terminal Domain: Binding Preferences Toward A and B Antigens With Different Peripheral Core Presentations. Frontiers in Chemistry, 9, 664097.

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NMR Analysis of Glycan Interactions

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The NMR experiments were acquired using an 800 MHz Bruker spectrometer with a cryoprobe (Bruker, Billerica, MA, United States). The ROESY spectra for the glycans were acquired in the presence of 50 μM Gal-4N with a 1:20 protein:ligand ratio in the corresponding deuterated PBS buffer at 298 K.

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NMR Spectroscopy of CARD Protein Domains

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All NMR spectra shown were collected in 50 mM HEPES, 300 mM NaCl, 0.5 mM TCEP, pH 7.0 at 37 °C on a Bruker 800 MHz Bruker Spectrometer with a cryogenically cooled probe. All were ¹⁵N-TROSY experiments, with the exception of the CARD9²⁻⁹⁷ spectrum in Fig. 1c, which was a ¹⁵N-HQSC. The CARD11^8–172 spectrum in Fig. 1b was collected at 150 μM, while the CARD9^2–152 and CARD9²⁻⁹⁷ spectra depicted in Fig. 1c were collected at 200 and 400 μM, respectively. The spectra depicted in Fig. 4 and Supplementary Fig. 2 were all collected at 200 μM using identical experimental parameters.

Holliday M.J., Witt A., Rodríguez Gama A., Walters B.T., Arthur C.P., Halfmann R., Rohou A., Dueber E.C, & Fairbrother W.J. (2019). Structures of autoinhibited and polymerized forms of CARD9 reveal mechanisms of CARD9 and CARD11 activation. Nature Communications, 10, 3070.

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Solid-state NMR Resonance Assignments

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NMR spectra were recorded on an 800 MHz Bruker spectrometer, equipped with a 3.2 mm E^free triple resonance (¹H-¹³C-¹⁵N) magic angle spinning (MAS) probe. The spinning frequency and temperature were actively controlled at 11.111 kHz and 5 °C, respectively. The sequential ¹³C and ¹⁵N resonance assignments were determined using a set of standard 2D and 3D chemical shift correlation experiments including: 2D ¹⁵N-¹³Cα (NCA), 2D ¹⁵N-¹³C’ (NCO), 2D ¹⁵N-¹³Cα-¹³CX (N(CA)CX), 2D ¹⁵N-¹³C’-¹³CX (N(CO)CX), 3D ¹⁵N-¹³Cα-¹³CX (NCACX), 3D ¹⁵N-¹³C’-¹³CX (NCOCX) and 3D ¹³Cα-¹⁵N-¹³C’-¹³CX (CAN(CO)CX). NMR spectra were processed with Bruker TopSpin 3.7 software and NMRPipe (Delaglio et al., 1995 (link)) and analyzed using Sparky (Goddard and Kneller 2006 ), and data were collected for several independent fibril preparations to confirm sample reproducibility.

Dao H., Hlaing M.Z., Ma Y., Surewicz K., Surewicz W.K, & Jaroniec C.P. (2020). 13C and 15N chemical shift assignments of A117V and M129V human Y145Stop prion protein amyloid fibrils. Biomolecular NMR assignments, 15(1), 45-51.

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NMR Experiments in Buffer Solution

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Nuclear magnetic resonance (NMR) experiments were performed in buffer containing 20 mM Tris, pH 7.0, 150 mM KCl, 1 mM EDTA, 1 mM DTT and 0.1 mM AEBSF, with 5% ²H₂O, except where noted. NMR data were collected on a 500 MHz Bruker spectrometer (Boston University School of Medicine), an 800 MHz Bruker spectrometer (Brandeis University) and an 850 MHz Bruker spectrometer (Brown University), all equipped with cryoprobes.

Nag N., Lin K.Y., Edmonds K.A., Yu J., Nadkarni D., Marintcheva B, & Marintchev A. (2016). eIF1A/eIF5B interaction network and its functions in translation initiation complex assembly and remodeling. Nucleic Acids Research, 44(15), 7441-7456.

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NMR Spectroscopy of Protein Samples

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All NMR spectra were recorded on an 800‐MHz Bruker spectrometer equipped with a TCI cryoprobe, in buffer containing 1.5 mM phosphate, 1.5 mM calcium, and sodium, 5% DMSO at pH 7 at 298 K. For NOESY spectra, the H₂O buffer was exchanged to D₂O buffer in the concentrator at 4°C. The NOESY spectra were collected with mixing times of 40, 70, 100, and 150 ms, processed with NMRPipe (Delaglio et al, 1995) and analyzed using CCPNmr analysis (Vranken et al, 2005).

Mariappan A., Soni K., Schorpp K., Zhao F., Minakar A., Zheng X., Mandad S., Macheleidt I., Ramani A., Kubelka T., Dawidowski M., Golfmann K., Wason A., Yang C., Simons J., Schmalz H., Hyman A.A., Aneja R., Ullrich R., Urlaub H., Odenthal M., Büttner R., Li H., Sattler M., Hadian K, & Gopalakrishnan J. (2018). Inhibition of CPAP–tubulin interaction prevents proliferation of centrosome‐amplified cancer cells. The EMBO Journal, 38(2), e99876.

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STD NMR Characterization of Lectin-Ligand Interactions

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All the STD NMR experiments were performed using an 800 MHz Bruker spectrometer with a cryoprobe (Bruker, Billerica, MA, United States). The samples were prepared in the corresponding deuterated buffer. The temperature was 288 K for every experiment. An amount of 50 μM of the lectin with 50 equivalents of the ligand was employed for every experiment except for lactose, for which a 1:70 ratio was used. The STD spectra were acquired with 1,024 scans, 2 s of saturation time using a train of 50 ms Gaussian-shaped pulses, and 3 s of relaxation delay. The spin-lock filter applied to remove the signals of the lectin was set at 40 ms. The on-resonance frequency was set for the aromatic region at 6.58 ppm, while the off-resonance frequency was set at 100 ppm.

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NMR Sample Preparation and Data Acquisition

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All NMR samples were prepared in NMR buffer containing 25 mM HEPES-d18, 50 mM NaCl, 10 mM MgCl₂ (pH 7.4) with addition of 5 to 10% D₂O. All samples were internally referenced with 2,2-dimethyl-2-silapentane-5-sulfonate (DSS). The final NMR sample concentrations ranged between 50 µM to 300 µM. NMR spectra were recorded in a temperature range from 278 K to 308 K on Bruker 600, 800, 900 and 950 MHz spectrometers. ¹H NMR spectra were recorded with jump-return-Echo^{80 (link)} and gradient-assisted excitation sculpting^{81 (link)} for water suppression. 2D ¹H,¹H-NOESY spectra were recorded with jump-return-Echo^{80 (link)} water suppression on a Bruker 800 MHz spectrometer at 288 K and mixing times of 150 ms. NMR data were collected, processed and analyzed using TopSpin 3.6.2 (Bruker) and Sparky 3.115^{82 (link)}.

Leisegang M.S., Bains J.K., Seredinski S., Oo J.A., Krause N.M., Kuo C.C., Günther S., Sentürk Cetin N., Warwick T., Cao C., Boos F., Izquierdo Ponce J., Haydar S., Bednarz R., Valasarajan C., Fuhrmann D.C., Preussner J., Looso M., Pullamsetti S.S., Schulz M.H., Jonker H.R., Richter C., Rezende F., Gilsbach R., Pflüger-Müller B., Wittig I., Grummt I., Ribarska T., Costa I.G., Schwalbe H, & Brandes R.P. (2022). HIF1α-AS1 is a DNA:DNA:RNA triplex-forming lncRNA interacting with the HUSH complex. Nature Communications, 13, 6563.

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NOESY NMR Analysis of RGDV-gemcitabine

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To reveal the manner of the molecular assembly of RGDV-gemcitabine, the NOESY 2D NMR spectrum was measured on Bruker 800 MHz spectrometer. The measurement was performed by following the procedure of the equipment.

Liu W., Mao Y., Zhang X., Wang Y., Wu J., Zhao S., Peng S, & Zhao M. (2019). RGDV-modified gemcitabine: a nano-medicine capable of prolonging half-life, overcoming resistance and eliminating bone marrow toxicity of gemcitabine. International Journal of Nanomedicine, 14, 7263-7279.

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