Founder & Director, mcalbyrne Ltd
Matthew Calthorpe‑Byrne
Dr Matthew Calthorpe-Byrne is a structural biologist and enzymologist who solves protein structures by cryo-EM and X-ray crystallography. He founded mcalbyrne Ltd in 2025 to build the software he wanted as a scientist — and the games he wanted to play.
Research
Currently a Postdoctoral Research Associate in the Siebold Group at the Division of Structural Biology (STRUBI), University of Oxford, which studies how Hedgehog and BMP morphogen signals are initiated, modulated and transduced at the cell surface.
- Publications
- 16
- Span
- 2013–25
- Selected venues
- Cell · Nature Comms · JACS · ACS Nano
Career
2011 — Present- 2026Current
Postdoctoral Research Associate
Siebold Group, Division of Structural Biology (STRUBI), University of Oxford
- 2025Current
Founder & Director
mcalbyrne Ltd
- 2025
EM Staff Scientist
eBIC, Diamond Light Source
- 2023
Senior Scientist
Exscientia
- 2021
EM Staff Scientist
eBIC, Diamond Light Source
- 2016
Postdoctoral Researcher
University of Leeds
- 2011
PhD
University of Bristol
Publications
16 of 16- 2025 Computational design of therapeutic antibodies with improved developability mAbs
- 2025 Dynamic assembly of pentamer-based protein nanotubes ACS Nano
- 2024 The cryoEM structure of the Hendra henipavirus nucleoprotein Scientific Reports
- 2024 Structure of the plant plastid-encoded RNA polymerase Cell
- 2023 CryoEM and stability analysis of virus-like particles of potyvirus and ipomovirus Communications Biology
- 2021 Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action Nature Communications
- 2021 The structure of a plant-specific partitivirus capsid Communications Biology
- 2021 A replicating viral vector greatly enhances accumulation of helical virus-like particles Viruses
- 2020 Nek7 conformational flexibility and inhibitor binding probed through protein engineering Biochemical Journal
- 2020 Structure and mechanism of a dehydratase/decarboxylase enzyme couple Scientific Reports
- 2019 Combining transient expression and cryo-EM to obtain high-resolution structures of luteovirid particles Structure
- 2019 A natural Diels–Alder biocatalyst enables efficient [4+2] cycloaddition ChemCatChem
- 2019 An esterase-like lyase catalyzes acetate elimination in spirotetronate biosynthesis Angewandte Chemie
- 2019 Affimer reagents as tools in diagnosing plant virus diseases Scientific Reports
- 2016 The catalytic mechanism of a natural Diels–Alderase revealed in molecular detail JACS
- 2013 Improving the success rate of protein crystallization by random microseed matrix screening JoVE
Links open the publisher's page, where full author lists are given.
From the bench
CryomaskR
The mask-building tool that came out of this work — now mcalbyrne's first scientific software product.