Using Collision Cross Section Distributions to Assess the Distribution of Collision Cross Section Values

In this study we explore the use of collision cross section distributions to allow comparability of IM-MS data for proteins on different instruments. We present measurements on seven standard proteins across three IM-MS configurations, namely an Agilent 6560 IM QToF, a Waters Synapt G2 possessing a TWIMS cell and a modified Synapt G2 possessing an RF confining linear field drift cell. Mobility measurements were taken using both He and N₂ as the drift gases. To aid comparability across instruments and best assess the corresponding gas-phase conformational landscapes of the protein ‘standards’ we present the data in the form of averaged collision cross section distributions.

Using Collision Cross Section Distributions to Assess the Distribution of Collision Cross Section Values

In this study we explore the use of collision cross section distributions to allow comparability of IM-MS data for proteins on different instruments. We present measurements on seven standard proteins across three IM-MS configurations, namely an Agilent 6560 IM QToF, a Waters Synapt G2 possessing a TWIMS cell and a modified Synapt G2 possessing an RF confining linear field drift cell. Mobility measurements were taken using both He and N₂ as the drift gases. To aid comparability across instruments and best assess the corresponding gas-phase conformational landscapes of the protein ‘standards’ we present the data in the form of averaged collision cross section distributions.

Using Collision Cross Section Distributions to Assess the Distribution of Collision Cross Section Values

In this study we explore the use of collision cross section distributions to allow comparability of IM-MS data for proteins on different instruments. We present measurements on seven standard proteins across three IM-MS configurations, namely an Agilent 6560 IM QToF, a Waters Synapt G2 possessing a TWIMS cell and a modified Synapt G2 possessing an RF confining linear field drift cell. Mobility measurements were taken using both He and N₂ as the drift gases. To aid comparability across instruments and best assess the corresponding gas-phase conformational landscapes of the protein ‘standards’ we present the data in the form of averaged collision cross section distributions.

Ion mobility mass spectrometry of peptide, protein, and protein complex ions using a radio-frequency confining drift cell

A new drift cell was used to measure collision cross sections and characterize the origins of ion mobility peak broadening for biological molecules and assemblies.