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. Author manuscript; available in PMC: 2017 Feb 15.
Published in final edited form as: Nat Chem. 2016 Aug 15;8(12):1152–1158. doi: 10.1038/nchem.2591

Figure 1.

Figure 1

Mass spectrum of ZMPSTE24 reveals zinc binding. (A) High-resolution Orbitrap QExactive mass spectrum of ZMPSTE24 released from a detergent (octyl glucose neopentyl glycol, OGNG) micelle. Adduct peaks at higher m/z are due to binding of lipids (POPG and cholesterol hemisuccinate) that co-purify with the protein. Inset: holo and apo-metallo ZMPSTE24 can be resolved (masses of 55579 Da and 55517 Da, respectively), confirming that Zn2+ is bound to the majority of the protein population.