Students prepared 1 L bacterial cultures to overexpress recombinant Goα protein, induced the cultures with IPTG, and harvested the cells the following day. Protein purification was performed in pairs, with students given 20 mL of lysed cells to filter and load in a Ni-NTA column. They purified His-MBP-GOα and subsequently removed the tag to isolate GOα. Quality was assessed by electrophoresis and intact mass analysis. At the end of the module, students learned to perform a protein concentration assay, analyze data, and create figures in Microsoft Excel. They also analyzed gels on Image Lab (). At the end of the purification module, a discussion was held to reinforce concepts and foster a collaborative workspace. Students presented their purification results and discussed pitfalls during expression and/or purification. Instructors presented potential scenarios and questions on protein expression and purification to assess students' ability to catch mistakes and to suggest viable solutions. This allowed students to communicate and apply the materials they learned.