Even though trained as an X-ray crystallographer, the author shares his experience on why and how he learned and engaged other biophysical techniques.The regulatory (R) subunit of protein kinase A (PKA) modulates the activity of PKA during translation of extracellular signals into a biological response in a cAMP-dependent manner. PKA exists in two distinct and structurally dissimilar conformations. In our work, we engaged X-ray crystallography, structural proteomics approaches, amide hydrogen/deuterium exchange and ion mobility mass spectrometry1.Hibiscus latent Singapore virus (HLSV) is a rigid rod-shaped plant virus and a new member of the Tobamovirus family. Unlike all other Tobamoviruses, the HLSV genome contains a unique poly(A) tract in its 3′ untranslated region which plays a crusial role in viral infection. We determined the structure of HLSV by X-ray fiber diffraction. The nucleotide recognition mechanism of HLSV during virus assembly is discussed2.Thioredoxins (Trxs) play a key role in maintaining a redox environment in the cell. They act as potential reducing agents and are also known to activate the DNA binding activity of NF-κB, an important transcription factor. In our work on 16-kDa Trx-like protein from Carcinoscorpius rotundicauda (Cr-TRP16), we solved the structure by NMR and explored the molecular basis of NF-κB activation using NMR, analytical ultracentrifugation and other techniques3.1. Badireddy, S. et al. (2011). Mol. Cell. Proteomics, 10:M110.004390.2. Tewary, S.K. et al. (2011). J. Mol. Biol., 406, 516-526.3. Giri, P.K. et al. (2012). J. Biol. Chem, 287, 29417-29428.