Cryo-EM Structure of CYP3A4: Unliganded and Substrate-Bound

This white paper presents a gene-to-structure cryo-EM study of CYP3A4, a cytochrome P450 enzyme central to drug metabolism. Follow the project from recombinant protein production and analytical characterization through grid screening, data collection, 3D reconstruction, and structural interpretation.

Examining CYP3A4 Structure with Cryo-EM

Although CYP3A4 has been studied extensively by X-ray crystallography, cryo-EM offers a complementary view of particle behavior, conformational flexibility, and oligomeric state in solution. The study examines the soluble domain of this 57 kDa target in both its unliganded form and in complex with hydroxychloroquine (HCQ), illustrating what can be learned from cryo-EM even for a relatively small and well-characterized protein.

What You’ll Learn in the White Paper

• How the CYP3A4 sample was expressed, purified, and assessed for cryo-EM
• How preferred orientation was addressed during grid screening and data collection
• What the unliganded and HCQ-bound reconstructions reveal about assembly and ligand binding

Download the white paper to explore the complete CYP3A4 cryo-EM workflow, structure figures, and study findings.