The Protein Crystallography group in the Hazra Lab focuses on understanding the structural basis of β-lactamase-mediated antibiotic resistance. Our research aims to unravel the three-dimensional architecture, catalytic mechanisms, and inhibitor interactions of clinically relevant β-lactamase enzymes using X-ray crystallography, biophysical approaches, and enzyme kinetics. Here, we employ the high-precisionautomated liquid-handling robotic platform Phoneix for protein crystallization trials, along with the Rigaku MicroMax HF-007 for crystal diffraction screening and X-ray diffraction data collection. The lab also works on structural characterization of β-lactamase insertion variants and point mutants to understand how sequence variations influence enzyme stability, substrate recognition, catalytic efficiency, and resistance profiles. By integrating protein purification, crystallization, diffraction data analysis, enzyme kinetics, and structure-guided studies, we seek to provide mechanistic insights into antibiotic resistance. In parallel, the lab is actively exploring novel therapeutic strategies by testing next-generation β-lactamase inhibitors, including boronic acid based compounds, to evaluate their efficiency as effective drugs against multidrug-resistant bacterial pathogens.