A method of ionising a sample is disclosed comprising nebulising a sample which includes monoclonal antibody (“mAb”) molecules. A stream of monoclonal antibody droplets or charged droplets is directed so as to impact upon a target or electrode so as to form intact parent monoclonal antibody ions, intact minus light chain parent monoclonal antibody ions or light chain (“LC”) fragment monoclonal antibody ions.

A mass spectrometer collision cell system, comprising: a gas containment vessel comprising an internal chamber having ion inlet and ion outlet ends and a cross-sectional area, A.sub.chamber; a gas inlet aperture; first and second gas outlet apertures that are disposed at or proximal to the ion inlet and outlet ends, respectively, and that have respective outlet aperture cross-sectional areas, A.sub.aperture1 and A.sub.aperture2, and an average outlet aperture cross-sectional area, A.sub.aperture.sup.ave; a longitudinal axis of the chamber extending from the ion inlet end to the ion outlet end and having a length, L.sub.chamber; and a set of multipole rod electrodes, at least a portion of each multipole rod electrode being within the chamber, wherein the values of A.sub.chamber, L.sub.chamber and A.sub.aperture.sup.ave are such that the combined gas conductance of the chamber and the gas outlet apertures is not greater than 95 percent of the gas conductance of the gas outlet apertures alone.

A method of producing ions from a sample is disclosed. The method comprises directing a spray of droplets onto a sample, and causing droplets comprising analyte from the sample to impact upon a surface so as to generate analyte ions.

The present disclosure relates to a method of identifying components present in a lipoprotein. Methods provided include single particle mass spectrometry, such as charge detection mass spectrometry (CDMS). Distinct subpopulations that exist within lipoprotein classes are determined by correlating m/z and mass.

The disclosure features systems and methods that include: exposing a biological sample to an ion beam that is incident on the sample at a first angle to a plane of the sample by translating a position of the ion beam on the sample in a first direction relative to a projection of a direction of incidence of the ion beam on the sample; after each translation of the ion beam in the first direction, adjusting a focal length of an ion source that generates the ion beam; and measuring and analyzing secondary ions generated from the sample by the ion beam after adjustment of the focal length to determine mass spectral information for the sample, where the sample is labeled with one or more mass tags and the mass spectral information includes populations of the mass tags at locations of the sample.

A method of ionising a sample is disclosed comprising nebulising a sample which includes first biomolecules such as bovine insulin comprising one or more disulphide (S—S) bonds. A stream of droplet or charged droplets comprising one or more disulphide (S—S) bonds is directed so as to impact upon a target (106) or electrode so as to cause the breaking of a portion of the disulphide bonds. Alternatively, charged droplets may pass through an electric field region determined by an electrode (106) arranged downstream of a nebuliser or electrospray probe and an ion inlet (104) of a mass spectrometer so as to cause the breaking of a portion of the disulphide bonds.

Devices and methods for surface-induced association are disclosed herein. According to one embodiment, a device for surface-induced dissociation (SID) includes a collision surface and a deflector configured to guide precursor ions from a pre-SID region to the collision surface. In some embodiments, an extractor extracts ions off the collision surface after collision with the collision surface. In some embodiments, an RF device can collect and/or transmit the extracted ions. In some embodiments, an ion funnel guides product ions resulting from collision with the collision surface to a post-SID region. Some aspects of the disclosure are directed to methods for surface-induced dissociation, which may in some embodiments include using of a split lens or an ion funnel.

The present disclosure relates to methods of identifying components present in intact lipoprotein particles. Methods provided include single particle mass spectrometry, such as charge detection mass spectrometry (CDMS). Distinct subtypes and subpopulations that exist within lipoprotein density classes are determined based on simultaneously measured m/z and charge of ionized lipoprotein particles.

The disclosure features systems and methods that include: exposing a biological sample to an ion beam that is incident on the sample at a first angle to a plane of the sample by translating a position of the ion beam on the sample in a first direction relative to a projection of a direction of incidence of the ion beam on the sample; after each translation of the ion beam in the first direction, adjusting a focal length of an ion source that generates the ion beam; and measuring and analyzing secondary ions generated from the sample by the ion beam after adjustment of the focal length to determine mass spectral information for the sample, where the sample is labeled with one or more mass tags and the mass spectral information includes populations of the mass tags at locations of the sample.

Mass spectrometry (MS) based systems and methods of implementing multi-stage MS/MS analysis for identification of experimental glycolipid samples. A processor communicatively coupled to a memory and a reference spectral database (1) implements a first stage analysis of glycan fragment data including determining, based on a matching reference glycan of a candidate reference glycolipid, a glycan structure of a glycan portion of the experimental glycolipid. The processor further (2) implements a second stage analysis of lipid/glycolipid fragment data including determining a lipid structure of a lipid portion of the experimental glycolipid by performing a spectral comparison of one or more MS/MS spectral values of a shifted experimental lipid fragment data with one or more MS/MS spectral values of matching reference lipid/glycolipid fragment data of the candidate reference glycolipid. A combination of the determined glycan structure and lipid structure gives the structure of each specific glycolipid in the experimental glycolipid sample.