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Native mass spectrometry, the method by which noncovalent protein complexes are retained in the gas phase for intact mass analysis, is gaining interest as a method for intact protein characterization. The development of a modified orbital ion trap platform for high-resolution analyses has expanded the role of native mass spectrometry to address the challenges of intact protein characterization. Here, we give an overview of the types of analyses that have recently been accomplished with this new instrumentation, ranging from highly decorated small proteins to large, noncovalent complexes that bind small-molecule ligands. These examples highlight the capabilities of native mass spectrometry and hint at the future role in intact protein characterization. [ABSTRACT FROM AUTHOR]

The article focuses on the development of cryo-electron microscopy (EM) that provide detailed crystallized structure of a molecule. Topics discussed include the use of electron detector technology to illuminate an image structure, the high-resolution structure of the single particle and the collection of microscopic images.