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Analysis of protein single crystal by IR-matrix-assisted laser desorption/ionization (CAT#: STEM-ST-0307-LJX)

Introduction

Lasers emitting in the ultraviolet wavelength range of 260-360 nm are almost exclusively used for matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of macromolecules. IR-MALDI of lyophilized proteins, air dried protein solutions, or protein crystals up to a molecular mass of 30 kDa is possible without the addition of any separate matrix.




Principle

In a very small area and a very short time interval (ns order of magnitude), the laser delivers high-intensity pulse energy to the sample under test, causing it to desorption and ionize instantaneously without thermal decomposition. MALDI is a mass spectrometry ionization method for direct evaporation and ionization of non-volatile samples.

Applications

For measuring the molecular weight of biological macromolecules, such as the molecular weight distribution of peptides, proteins, nucleic acids, polymers and oligomer analysis.

Procedure

1. Mix the sample with the appropriate matrix material and load it onto the metal plate.
2. Pulsed laser light is used to irradiate the sample and trigger ablation and desorption of the sample and matrix materials.
3. Analyte molecules are ionized by protonation or deprotonation in the thermal plume of the ablated gas and are then accelerated to a mass analyzer for analysis.

Materials

• Sample Type:
Protein single crystal

Notes

1. During shutdown, if the nitrogen is not turned off, the pressure should be properly lowered to avoid moisture.
2. Keep an eye on instrument drift during manual measurement. If there is drift, the instrument needs to be calibrated with standard peptide or standard protein.
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