Protocol detail

Spectroscopic Analysis of Protein Interactions

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Absorption measurements were carried out at 20.0 ± 0.5 °C using a Varian (Palo Alto, CA, USA) CARY400 spectrophotometer. All spectra were corrected for buffer contributions. Fluorescence emission spectra were collected using a FluoroMax-3 fluorometer (HORIBA Jobin Yvon, Kyoto, Japan) at 20 ± 0.5 °C, equilibrating samples for 5 min prior to spectra acquisition. CysE/CdiA-CT stoichiometric binding to CysK was monitored by measuring PLP fluorescence emission at 500 nm following excitation at 412 nm (see [24 (link)]) [39 (link),50 (link),51 (link)]. All spectra were corrected for buffer contribution, and the slit width set to optimize the signal-to-noise ratio.

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Rosa B., Marchetti M., Paredi G., Amenitsch H., Franko N., Benoni R., Giabbai B., De Marino M.G., Mozzarelli A., Ronda L., Storici P., Campanini B, & Bettati S. (2019). Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action. International Journal of Molecular Sciences, 20(20), 5219.

Publication 2019

CARY400 spectrophotometer FluoroMax-3 fluorometer

Buffer Fluorescence

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Variable analysis

independent variables

Temperature: 20.0 ± 0.5 °C

dependent variables

Absorption spectra
Fluorescence emission spectra
PLP fluorescence emission at 500 nm following excitation at 412 nm

control variables

Cary400 spectrophotometer used for absorption measurements
FluoroMax-3 fluorometer used for fluorescence emission spectra
Samples equilibrated for 5 min prior to spectra acquisition
Spectra corrected for buffer contributions

controls

Positive control: None specified
Negative control: None specified

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