Abstract
Mass spectrometry is often used to ascertain the accurate mass of purified protein samples prior to crystallization screening. However, in many cases data regarding the form of the protein crystallizing can also be useful, as this may differ from the original sample. Development of a simple method for the preparation and mass spectrometry of crystal-derived protein samples is described. The method is exemplified by the determination of the phosphorylation state of protein in a crystal derived from a mixture of phosphorylated and unphosphorylated protein.
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