Rachel Johnson PhD

Senior Protein Scientist and Cryo-EM Specialist

Rachel Johnson has significant expertise in Cryo-EM gained from academia and industry.

Rachel Johnson PhD

More about Rachel

Rachel began her scientific studies at the University of Leeds where she obtained an MChem degree in Medicinal Chemistry. During her final year structure-based drug design project, she became particularly interested in how small molecule ligands interact with their target protein and how these interactions could guide the design of the next generation of compounds. In 2015, Rachel began her PhD project within the Astbury centre at the University of Leeds where she learned more about the biochemistry/structural biology side of the drug discovery pipeline. The focus of her PhD was the use of cryo-EM to support drug discovery programs. Here, she was able to determine cryo-EM structures of multiple membrane proteins that ranged in molecular weight from ~100 kDa to 1 MDa.

After completing her PhD, Rachel moved to Melbourne to undertake a postdoctoral position at the Monash Institute of Pharmaceutical Sciences (MIPS) where she purified and obtained high resolution cryo-EM structures of G Protein Coupled Receptors (GPCRs). Here, she particularly enjoyed determining structures for GPCRs with small molecule ligands bound. In some cases, she was even able to see the water network surrounding the ligand thus providing important information to the chemists to drive the design of future compounds. After almost three years in Australia, Rachel returned to the UK as a Senior Scientist at OMass Therapeutics, Oxford. Rachel is now excited to move back to the North of England and to join Peak Proteins. She is looking forward to using her cryo-EM skills and knowledge in a CRO setting where she is aiming to obtain high resolution structures for a wide range of proteins.

Outside of work, Rachel enjoys walks in the countryside and playing badminton with friends. She has also recently enjoyed caring for plants and is trying to grow succulents and Bonsai trees from seed.

A structural basis for amylin receptor phenotype.
Cao, J., Belousoff, M. J., Liang, Y. L., Johnson, R. M., et al.
Science, 2022, 375 (6587), eabm9609.

Cryo-EM structure of the dual incretin receptor agonist, peptide-19, in complex with the glucagon-like peptide-1 receptor.
Johnson, R. M., Zhang, X., Piper, S. J., et al.,
Biochemical and Biophysical Research Communications 2021, 578, 84-90.

Evolving cryo-EM structural approaches for GPCR drug discovery
Zhang, X., Johnson, R. M., Drulyte, I., et al.,
Structure 2021, 29 (9), 963-974. e6.

Approaches to altering particle distributions in cryo-electron microscopy sample preparation.
Drulyte, I., Johnson, R. M., Hesketh, E. L., et al.,
Acta Crystallographica Section D: Structural Biology 2018, 74 (6), 560-571.

Membranes under the magnetic lens: A dive into the diverse world of membrane protein structures using cryo-EM.
Piper, S. J., Johnson, R. M., Wootten, D., Sexton, P. M.,
ACS Chemical Reviews, 2022, 122 (17), 13989-14017.

Structural insight into selectivity of amylin and calcitonin receptor agonists.
Cao, J., Belousoff, M.J., Gerrard, E., …, Johnson, R.M., Wootten, D., Sexton, P.M.
Nat Chem Biol, 2023.

X-ray and cryo-EM structures of inhibitor-bound cytochrome bc1 complexes for structure-based drug discovery.
Amporndanai, K., Johnson, R. M., O'Neill, P. M., et al.,
IUCrJ 2018, 5 (2), 200-210.

Human TRPC5 structures reveal interaction of a xanthine-based TRPC1/4/5 inhibitor with a conserved lipid binding site.
Wright, D. J., Simmons, K. J., Johnson, R. M., et al.,
Communications biology 2020, 3 (1), 1-11.

Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo–electron microscopy.
Gopalasingam, C. C., Johnson, R. M., Chiduza, G. N., et al.,
Science advances 2019, 5 (8), eaax1803.

New insights into the structure and function of class B1 GPCRs.
Cary, B. P., Zhang, X., Cao, J., Johnson, R. M., et al.,
Endocrine Reviews, 2023, 44 (3), 492-517.

The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer.
Jamali, M. A. M., Gopalasingam, C. C., Johnson, R. M., et al.,
IUCrJ 2020, 7 (3), 404-415.

A structurally characterized Staphylococcus aureus evolutionary escape route from treatment with the antibiotic linezolid.
Perlaza-Jiménez, L., Tan K., Piper, S. J., Johnson, R. M., et al.
Microbiology Spectrum, 2022, 10 (4), e00583-22.

Cryo-EM structure and molecular dynamics analysis of the fluoroquinolone resistant mutant of the AcrB transporter from Salmonella.
Johnson, R. M., Fais, C., Parmar, M., et al.
Microorganisms 2020, 8 (6), 943.

Structure-based identification and characterization of inhibitors of the epilepsy-associated KNa1.1 (KCNT1) potassium channel
Cole, B. A., Johnson, R. M., Dejakaisaya, H., et al.,
IScience 2020, 23 (5), 101100.

Potent tetrahydroquinolone eliminates apicomplexan parasites.
McPhillie, M. J., Zhou, Y., Hickman, M. R., Gordon, J. A., Weber, C. R., Li, Q., Lee, P. J.,  Amporndanai, K., Johnson, R. M., et al.
Frontiers in cellular and infection microbiology 2020, 10, 203.

LAT1 (SLC7A5) and CD98hc (SLC3A2) complex dynamics revealed by single-particle cryo-EM.
Chiduza, G. N., Johnson, R. M., Wright, G. S., et al.,
Acta Crystallographica Section D: Structural Biology 2019, 75 (7), 660-669.

Emerging role of electron microscopy in drug discovery.
Johnson, R. M., Higgins, A. J., Muench, S. P.,
Trends in biochemical sciences 2019, 44 (10), 897-898.

In silico fragment-based design identifies subfamily B1 metallo-β-lactamase inhibitors.
Cain, R., Brem, J. R., Zollman, D., McDonough, M. A., Johnson, R. M., et al.
Journal of medicinal chemistry 2018, 61 (3), 1255-1260.

The Growing Role of Electron Microscopy in Anti-parasitic Drug Discovery.
Johnson, R. M., Rawson, S., McPhillie, M. J., et al.,
Current medicinal chemistry 2018, 25 (39), 5279-5290.

Structural Biology Team