Understanding the structure and interactions of native protein complexes is crucial for elucidating their mechanisms, potentially leading to innovative drug strategies for treating human diseases. However, their intrinsic and extrinsic heterogeneity and increasing size pose significant characterization challenges. Charge detection mass spectrometry (CDMS) using an electrostatic linear ion trap (ELIT) is a cutting-edge technique for ultra-high mass analysis. It simultaneously measures the mass-to-charge ratio (m/z) and charge (z) of individual ions, enabling mass calculation. In this work, we describe the use of a novel heated inlet for activating various native protein complexes, resulting in their structural elucidation and conformational characterization. This advancement enhances our understanding of complex biological systems and supports the development of targeted therapeutic strategies.