Richard Kirian

About

Dr. Richard Kirian is an Associate Professor in the Department of Physics at Arizona State University, with additional affiliations including the Biodesign Beus CXFEL Lab, the Center for Biological Physics, and the Biodesign Center for Applied Structural Discovery. His primary research focuses on the field of x-ray free-electron laser science, where he develops experimental measurement and diffraction analysis techniques for static and time-resolved studies of biological macromolecules. His work involves advancing three main techniques: femtosecond serial crystallography, time-resolved solution scattering, and single-molecule imaging. Dr. Kirian also develops particle injection systems for biomolecules and innovates new lensless diffractive imaging techniques. He earned his Ph.D. in physics from Arizona State University in 2011 and completed postdoctoral work at the Center for Free-Electron Lasers in Hamburg from 2011 to 2014. His research contributions include imaging single cells with X-ray lasers, developing aerosol injectors for single-particle diffractive imaging, and direct phasing of finite crystals illuminated with free-electron lasers. His expertise areas include the physics of biological systems and soft matter physics.

Research topics

• Computer Science
• Optics
• Chemistry
• Materials science
• Physics
• Nanotechnology
• Crystallography
• Biochemistry
• Biology
• Chromatography

Selected publications

• Megahertz single-particle imaging at the European XFEL

  Communications Physics · 2020 · 94 citations

  The emergence of high repetition-rate X-ray free-electron lasers (XFELs) powered by superconducting accelerator technology enables the measurement of significantly more experimental data per day than was previously possible. The European XFEL is expected to provide 27,000 pulses per second, over two orders of magnitude more than any other XFEL. The increased pulse rate is a key enabling factor for single-particle X-ray diffractive imaging, which relies on averaging the weak diffraction signal fr…

  DOI

• 3D diffractive imaging of nanoparticle ensembles using an x-ray laser

  Optica · 2020 · 79 citations

  Single particle imaging at x-ray free electron lasers (XFELs) has the potential to determine the structure and dynamics of single biomolecules at room temperature. Two major hurdles have prevented this potential from being reached, namely, the collection of sufficient high-quality diffraction patterns and robust computational purification to overcome structural heterogeneity. We report the breaking of both of these barriers using gold nanoparticle test samples, recording around 10 million diffra…

  DOI

• Segmented flow generator for serial crystallography at the European X-ray free electron laser

  Nature Communications · 2020 · 44 citations

  Serial femtosecond crystallography (SFX) with X-ray free electron lasers (XFELs) allows structure determination of membrane proteins and time-resolved crystallography. Common liquid sample delivery continuously jets the protein crystal suspension into the path of the XFEL, wasting a vast amount of sample due to the pulsed nature of all current XFEL sources. The European XFEL (EuXFEL) delivers femtosecond (fs) X-ray pulses in trains spaced 100 ms apart whereas pulses within trains are currently s…

  DOI

• In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors

  Nature Communications · 2020 · 39 citations

  Sleeping sickness is a fatal disease caused by the protozoan parasite Trypanosoma brucei (Tb). Inosine-5'-monophosphate dehydrogenase (IMPDH) has been proposed as a potential drug target, since it maintains the balance between guanylate deoxynucleotide and ribonucleotide levels that is pivotal for the parasite. Here we report the structure of TbIMPDH at room temperature utilizing free-electron laser radiation on crystals grown in living insect cells. The 2.80 Å resolution structure reveals the p…

  PublisherOA PDFDOI

• Co-flow injection for serial crystallography at X-ray free-electron lasers

  Journal of Applied Crystallography · 2021 · 24 citations

  Serial femtosecond crystallography (SFX) is a powerful technique that exploits X-ray free-electron lasers to determine the structure of macro-molecules at room temperature. Despite the impressive exposition of structural details with this novel crystallographic approach, the methods currently available to introduce crystals into the path of the X-ray beam sometimes exhibit serious drawbacks. Samples requiring liquid injection of crystal slurries consume large quantities of crystals (at times up…

  PublisherOA PDFDOI

Recent grants

• ABI Innovation: New Algorithms for Biological X-ray Free Electron Laser Data

  NSF · $762k · 2016–2020

• CAREER: Imaging dynamic macromolecules in solution with x-ray lasers

  NSF · $1.1M · 2020–2027

Frequent coauthors

• Henry N. Chapman

  Max Planck Institute for the Structure and Dynamics of Matter

  357 shared

• Anton Barty

  191 shared

• Jochen Küpper

  Center for Free-Electron Laser Science

  129 shared

• Kenneth R. Beyerlein

  Institut National de la Recherche Scientifique

  124 shared

• Salah Awel

  117 shared

• Richard Bean

  European X-Ray Free-Electron Laser

  116 shared

• Oleksandr Yefanov

  114 shared

• Daniel A. Horke

  110 shared

Labs

• Biodesign Beus CXFEL LabPI

  Develops experimental measurement and diffraction analysis techniques for static and time-resolved studies of biological macromolecules.

Education

• Ph.D., Physics

  Arizona State University

  2011

• B.A., Astronomy

  University of California-Berkeley

  2006

• B.A., Physics

  University of California-Berkeley

  2006

Similar researchers at Arizona State University

• Jingyue Liuh-74
• Stuart Lindsayh-63
• Andrei Belitskyh-52