Advance 700

Manufactured by Bruker

Sourced in United States

The Advance 700 is a high-performance nuclear magnetic resonance (NMR) spectrometer designed for advanced research applications. It features a 700 MHz superconducting magnet and provides superior spectral resolution and sensitivity for the analysis of complex samples.

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Lab products found in correlation

Drx 600, by Bruker (2 mentions) Elemental analyser vario macro chn, by Elementar (1 mentions) Ramanmicro 200 spectrometer, by PerkinElmer (1 mentions) Spectrum 2000, by PerkinElmer (1 mentions)

5 protocols using advance 700

Investigating PKIα Intramolecular Dynamics

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The intra-molecular ¹H PRE-Γ₂ relaxation measurements on the free form of PKIα mutants were carried out using the pulse sequence by Iwahara et al. (2007) (link) on a Bruker Advance 700 MHz spectrometer at 27°C. All experiments were performed using 160 scans with 2048 (¹H) and 128 (¹⁵N) complex points. A two-time point measurement was performed using a relaxation time of 4 and 14 ms in an interleaved fashion. The ¹H PRE-Γ₂ values were calculated using the equation (Iwahara et al., 2007 (link)):

Γ_{2} = \frac{1}{T_{b} - T_{a}} \ln \frac{I_{d i a} (T_{b}) I_{p a r a} (T_{a})}{I_{d i a} (T_{a}) I_{p a r a} (T_{b})}

where Γ2 is the PRE-relaxation rate, the time points are T_a and T_b, I_para is the corresponding intensity with a spin label and I_dia is the corresponding intensity with a reduced spin label:

σ (Γ_{2}) = \frac{1}{T_{b} - T_{a}} \sqrt{{\{\frac{σ_{d i a} (T_{a})}{I_{d i a} (T_{a})}\}}^{2} + {\{\frac{σ_{d i a} (T_{b})}{I_{d i a} (T_{b})}\}}^{2} + {\{\frac{σ_{p a r a} (T_{a})}{I_{p a r a} (T_{a})}\}}^{2} {+ \{\frac{σ_{p a r a} (T_{b})}{I_{p a r a} (T_{b})}\}}^{2}}

Where σ_dia and σ_para are the roots mean square noise of the respective spectra. For the simultaneous detection of inter- and intra-molecular PREs of PKIα bound to PKA-C/ATPγN, we used a TROSY-based CCLS variation of the standard PRE pulse sequence (Olivieri et al., 2018 (link)). For both paramagnetic and diamagnetic experiment, the complex sample was prepared with a total protein concentration of 140 μM using a 1:1 PKA-C/PKIα molar ratio.

Olivieri C., Wang Y., Li G.C., V S M., Kim J., Stultz B.R., Neibergall M., Porcelli F., Muretta J.M., Thomas D.D., Gao J., Blumenthal D.K., Taylor S.S, & Veglia G. (2020). Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. eLife, 9, e55607.

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NMR Analysis of DNA Structure and Thermodynamics

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NMR spectra were recorded on Bruker Advance 700, 850 and 950 MHz spectrometers equipped with cryogenically cooled probes. Experiments were performed at 37°C. For solution NMR, standard 3 mm NMR tubes were used. The samples were prepared in 1× buffer with 10% D₂O added for the lock. The concentration of DNA samples was between 0.35 and 2 mM. ¹⁵N and ¹³C HSQC experiments were performed using fully-labelled samples or with 5% low-enrichment ¹⁵N, ¹³C site-specific labeling for assignment of imino protons. To unambiguously assign the intranucleotide exchangeable imino to the nonexchangeable purine H8 and pyrimidine H6 protons through-bond connectivities, we used a HCCNH-TOCSY spectrum in uniformly {¹³C, ¹⁵N}-labeled DNA (37 (link),38 (link)). Melting experiments were performed using 500 μM of oligonucleotides. The NMR tube was put into the spectrometer at a start temperature of 4°C (277K). After 5 min, enough time for temperature stabilization, a 1H spectrum was recorded. The same process was repeated at increasing temperatures until a maximum temperature of 60°C (333 K) was reached.

Marquevielle J., Robert C., Lagrabette O., Wahid M., Bourdoncle A., Xodo L.E., Mergny J.L, & Salgado G.F. (2020). Structure of two G-quadruplexes in equilibrium in the KRAS promoter. Nucleic Acids Research, 48(16), 9336-9345.

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NMR Characterization of TAX1BP1-Ubiquitin Binding

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Wild-type TAX1BP1 zinc finger domain samples were prepared for NMR spectroscopy experiments in 1.0 mM in 90% H₂O and 10% D₂O in PBS containing 10 mM β-mercaptoethanol. All spectra were acquired with either a Bruker Advance 700 or a DRX600 spectrometer at 20°C, and referenced relative to external sodium 2,2-dimethyl-2-silapentane-5-sulfonate (DSS) for proton and carbon signals, or liquid ammonium for nitrogen. Assignments were obtained by standard NMR methods using ¹³C/¹⁵N-labeled and ¹⁵N-labeled samples. To map the binding interface between the TAX1BP1 zinc fingers and ubiquitin, we collected a series of ¹H-¹⁵N HSQC spectra of the ¹⁵N-labelled TAX1BP1 zinc finger domain in the presence of increasing molar ratios of unlabelled ubiquitin; a reciprocal titration was carried out with the unlabelled TAX1BP1 zinc finger domain added to ¹⁵N-labelled ubiquitin. Dissociation constants were obtained by fitting the concentration dependence of the normalized chemical shift changes to a single site-binding model. The coordinates and the NMR restraints have been deposited in the PDB with the codes PDB: 5aas and r5aasmr, respectively.

Tumbarello D.A., Manna P.T., Allen M., Bycroft M., Arden S.D., Kendrick-Jones J, & Buss F. (2015). The Autophagy Receptor TAX1BP1 and the Molecular Motor Myosin VI Are Required for Clearance of Salmonella Typhimurium by Autophagy. PLoS Pathogens, 11(10), e1005174.

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NMR Spectroscopy of NDP52 Zinc Finger

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NDP52 zinc finger domain samples for NMR spectroscopy experiments were typically at 1.0 mM in 90% H₂O and 10% D₂O in PBS containing 10 mM 2‐mercaptoethanol. All spectra were acquired with either a Bruker Advance 700 or a DRX600 spectrometer at 20°C and referenced relative to external sodium 2,2‐dimethyl‐2‐silapentane‐5‐sulfonate (DSS) for proton and carbon signals, or liquid ammonium for nitrogen. Assignments were obtained using standard NMR methods using ¹³C/¹⁵N‐labeled and ¹⁵N‐labeled samples. Distance constraints were derived from 2D NOESY spectra recorded on 1.5 mM samples with a mixing time of 100 ms. The three‐dimensional structure of the domain was calculated using the standard torsion angle dynamics‐simulated annealing protocol in the program CNS 1.2. Structures were accepted where no distance violation was > 0.25 Å and no dihedral angle violations > 5°. To map the binding interface between the NDP52 zinc finger and ubiquitin, a series of ¹H‐¹⁵N HSQC spectra of ¹⁵N‐labeled zinc finger domain in the presence of increasing molar ratios of unlabeled ubiquitin were recorded; a reciprocal titration was carried out with the unlabeled zinc finger domain added to ¹⁵N‐labeled ubiquitin. Dissociation constants were obtained by fitting the concentration dependence of the normalized chemical shift changes to a single site‐binding model.

Thurston T.L., Boyle K.B., Allen M., Ravenhill B.J., Karpiyevich M., Bloor S., Kaul A., Noad J., Foeglein A., Matthews S.A., Komander D., Bycroft M, & Randow F. (2016). Recruitment of TBK1 to cytosol‐invading Salmonella induces WIPI2‐dependent antibacterial autophagy. The EMBO Journal, 35(16), 1779-1792.

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Spectroscopic Analysis of Synthesized Compounds

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The vibrational spectra of the synthesized compounds (crystals) were registered using: (a) IR spectrophotometry (Perkin Elmer Spectrum 2000 FTIR spectrophotometer (PerkinElmer Inc., Waltham, MA, USA) (400–4000 cm⁻¹ range, KBr pellets)), and (b) Raman spectroscopy (RamanMicro 200 spectrometer (PerkinElmer Inc., Waltham, MA, USA)). The Raman spectra were recorded using a laser with the wavelength 785 nm, with a maximum power of 350 mW, in the range 200–3200 cm⁻¹, with a 20 × 0.40/FN22 objective lens and an exposure time of 15 s each time. The ¹³C NMR spectra in the solid phase were recorded on a Bruker Advance 700 (Madison, WI, USA) 700 MHz spectrometer, with a spectral width of 76,923.08 Hz and 4096 complex points. Elemental analyses were performed on an Elemental AnalyserVario Macro CHN (ElementarAnalysensysteme GmbH, Langenselbold, Germany).

Kubiak B., Muzioł T., Wrzeszcz G., Radtke A., Golińska P., Jędrzejewski T., Wrotek S, & Piszczek P. (2024). Structural Characterization and Bioactivity of a Titanium(IV)-Oxo Complex Stabilized by Mandelate Ligands. Molecules, 29(8), 1736.

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