Measurements were carried out on a Bruker UltrafleXtreme MALDI-TOF mass spectrometer (Bruker Daltonics, Bremen, Germany). First, the buffer and salt components from the samples of PVY virus and VLP constructs were exchanged with pure water, and samples were concentrated to 1.5 to 3.0 mg/ml with centrifugation through 10-kDa cutoff membranes. Samples were then mixed with saturated solution of sinapinic acid in a mixture of acetonitrile and 0.1% trifluoroacetic acid (1:1, v/v) in a 1:1 (v/v). One microliter of this solution was spotted on the target plate (dried-droplet method). The linear positive ion mode was used to acquire the mass spectra of the samples. The calibration was done externally using protein calibration standards I and II (Bruker Daltonics). Sample preparation procedure for the standards was the same as that for other samples. The standards were spotted on the nearest neighboring positions.
Protein calibration standards 1 and 2
Manufactured by Bruker
Sourced in Germany
Protein calibration standards I and II are reference materials used to calibrate and validate the performance of instruments and methods for the analysis of proteins. These standards provide a consistent and reliable way to ensure the accuracy and precision of protein measurements.
Automatically generated - may contain errors
2 protocols using protein calibration standards 1 and 2
1
MALDI-TOF Mass Spectrometry of Viral Proteins
2
MALDI-TOF MS Analysis of Intact Proteins
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The MALDI-TOF MS analyses were performed using chemicals at the highest commercially available purity supplied by Fluka Feinchemikalien (a subsidiary of Sigma-Aldrich, NeuUlm, Germany). Ground steel targets (Bruker Daltonik, Bremen, Germany) were used for sample deposition and the sinapinic acid was employed as matrix for MALDI analysis of intact proteins (dried droplet method) [28 (link)]. Protein Calibration Standards I and II (Bruker Daltoniks, Bremen, Germany) were used for external calibration. All the MS spectra were obtained using the MALDI-TOF/TOF mass spectrometer (Bruker Daltonik, Bremen, Germany) equipped with a modified neodymium-doped yttrium aluminum garnet (Nd:YAG) laser operating at the wavelength of 355 nm and frequency of 2 kHz. The system was controlled using the Bruker Daltonik software (flexControl and flexAnalysis). MS spectra of intact proteins were obtained in the linear positive mode in an m/z range of 15,000–30,000, applying an acceleration voltage of 25 kV. All mass spectra were acquired and processed using dedicated software flexControl and flexAnalysis, respectively (both from Bruker Daltonik).
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