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Microflex lrf spectrometer

Manufactured by Bruker

The Microflex LRF spectrometer is a compact and robust lab equipment designed for matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry analysis. It provides high-performance and reliable data acquisition capabilities for a wide range of applications.

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2 protocols using microflex lrf spectrometer

1

Comprehensive Nanomaterial Characterization Protocol

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Elemental analyses and electrospray-ionisation mass spectrometry (ESI-MS) were conducted at the analysis centre of Hokkaido University. The 1H NMR and 1H-1H COSY NMR spectra were acquired on a JEOL ECZ-400S or EX-270 spectrometer. Energy dispersive XRF spectra were acquired on a JEOL JSX-3100RII spectrometer using a Rh target. DLS analyses were conducted using an OTSUKA ELSZ-1000SCl analyser. Nitrogen and methanol vapour adsorption isotherms were measured using an automatic BELSORP-max (MicrotracBEL Co.) volumetric adsorption apparatus. Pore-size distributions were calculated using the density functional theory (DFT) method (DFT kernel: N2 at 77 K on silica, cylindrical pores, and NLDFT equilibrium model). Thermogravimetry-differential thermal analysis (TG-DTA) measurements were recorded using a Rigaku Thermoplus EVO TG-DTA 8120 with Al sample pans under an Ar flow. Matrix-assisted laser desorption/ionisation mass spectrometry (MALDI-MS) was conducted using a Bruker Microflex LRF spectrometer in a linear mode.
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2

Mapping TEFM Binding Site via Cross-Linking

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To map the TEFM binding site, EC-TEFM complex (5 μM in 40 mM Na-HEPES pH 7.5) was treated with a mixture of DSG/[2H4]-DSG (0.6 mM DMSO solution, ProteoChem) and the products of the reaction separated using 7% Tris-glycine SDS PAGE. The cross-linked species were excised from the gel and subjected to trypsin digestion in 100 mM NH4HCO3 buffer overnight at 37°C. The products of the digestion r eaction were extracted from the gel with CH3CN-0.1% TFA in water (9:1), dried in vacuum, re-dissolved in 10 mg/ml CHCA matrix in CH3CN-0.1% TFA in water (1:1), and the resulting solution applied on target for MALDI-TOF mass spectrometry. Mass spectra were taken on a MicroFlex LRF spectrometer (Bruker). Positively charged ions (M+H+) were analyzed in the reflector mode (m/z 1000 to 4000) and cross-linked peptides identified using xBobcat mass matching search engine (http://prottools.ethz.ch/orinner/public/htdocs/xquest/index_review.html) (Rinner et al., 2008 (link)).
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