Michael A Hough

Enzyme catalysis captured using multiple structures from one crystal at varying temperatures.

Resolving polymorphs and radiation-driven effects in microcrystals using fixed-target serial synchrotron crystallography.

Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins.

High-throughput structures of protein-ligand complexes at room temperature using serial femtosecond crystallography.

Successful sample preparation for serial crystallography experiments.

Serial Femtosecond Zero Dose Crystallography Captures a Water-Free Distal Heme Site in a Dye-Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in Fe =O Formation.

Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis.

Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of Fe = O formation in bacterial dye-decolorizing peroxidases.

Crystal structure of thermally stable homodimeric cytochrome c'-β from Thermus thermophilus.

Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature.

Serial femtosecond crystallography approaches to understanding catalysis in iron enzymes.

Serial Femtosecond Crystallography Reveals the Role of Water in the One- or Two-Electron Redox Chemistry of Compound I in the Catalytic Cycle of the B-Type Dye-Decolorizing Peroxidase DtpB.

Perspective: Structure determination of protein-ligand complexes at room temperature using X-ray diffraction approaches.

A heme pocket aromatic quadrupole modulates gas binding to cytochrome c'-β: Implications for NO sensors.

Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi.

The CCP4 suite: integrative software for macromolecular crystallography.

New insights into controlling radical migration pathways in heme enzymes gained from the study of a dye-decolorising peroxidase.

Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features.