Sam Horrell

Sam Horrell graduated from the University of Leicester in 2011 with a degree in Medical Biochemistry (BSc), he then moved to the University of Liverpool for a joint PhD project with Diamond Light Source; where he worked on method development for long wavelength phasing experiments, developed the multiple structures from one crystal (MSOX) technique, and studied the reaction mechanisms of EAL domain proteins from Pseudomonas aeruginosa. After a postdoc position at the University of Essex with the Hough group further developing the MSOX technique. Sam joined the Pearson lab in Hamburg in April 2017 to help design and construct the P14-2 Time resolved X-ray Crystallography (TREXX) end station. Sam joined Diamond Light Source in November 2019 as a postdoc on the microfocus beamline - I24, and is now a beamline scientist at I24 developing serial cystallography methods for synchrotrons and XFELs and investigating photo-induced promiscuity in ketoreductases. 

I work with several groups outside Diamond as part of my research. These include:

A list of my publications can be found below:

• Structural biology of SARS-CoV-2 endoribonuclease NendoU (nsp15)
• xia2.multiplex: a multi-crystal data-analysis pipeline
• 3DBionotes COVID-19 edition
• Making the invisible enemy visible
• Fixed Target Serial Data Collection at Diamond Light Source
• Homogeneous batch micro-crystallization of proteins from ammonium sulfate
• Open Science Discovery of Oral Non-Covalent SARS-CoV-2 Main Protease Inhibitor Therapeutics
• Liquid application method for time-resolved analyses by serial synchrotron crystallography
• A microfluidic flow-focusing device for low sample consumption serial synchrotron crystallography experiments in liquid flow 
• Enzyme catalysis captured using multiple structures from one crystal at varying temperatures
• Recent structural insights into the function of copper nitrite reductases 
• Active-site protein dynamics and solvent accessibility in native Achromobacter cycloclastes copper nitrite reductase
• Photoreduction and validation of haem–ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction
• Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases
• Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal
• Visualization of membrane protein crystals in lipid cubic phase using X-ray imaging