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Structural enzymology using X-ray free electron lasers.

Christopher Kupitz1, Jose L Olmos2, Mark Holl3

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This summary is machine-generated.

Mix-and-inject serial crystallography (MISC) enables studying enzyme reactions at room temperature with high time resolution. This study demonstrates MISC feasibility at an X-ray free electron laser for enzyme structural dynamics.

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Area of Science:

  • Structural Biology
  • Biochemistry
  • X-ray Crystallography

Background:

  • Mix-and-inject serial crystallography (MISC) is a technique for imaging enzyme-catalyzed reactions.
  • It offers advantages like room temperature structures, high time resolution (microseconds to seconds), and convenient reaction initiation.
  • Femtosecond X-ray pulses separate radiation damage from chemical processes.

Purpose of the Study:

  • To demonstrate the feasibility of MISC at an X-ray free electron laser (XFEL).
  • To study the reaction mechanism of *Mycobacterium tuberculosis* ß-lactamase with ceftriaxone.
  • To advance time-resolved structural dynamics studies of substrate-triggered biological reactions.

Main Methods:

  • Utilized mix-and-inject serial crystallography (MISC) with microcrystals of *M. tuberculosis* ß-lactamase.
  • Mixed enzyme microcrystals with ceftriaxone antibiotic solution.
  • Probed crystal structures using femtosecond X-ray pulses at an XFEL.

Main Results:

  • Obtained electron density maps for apo-ß-lactamase at 2.8 Å resolution.
  • Determined the structure of the ceftriaxone-bound ß-lactamase at 2.4 Å resolution.
  • Demonstrated MISC is effective for capturing enzyme-substrate interactions.

Conclusions:

  • MISC is a viable technique at XFELs for time-resolved structural studies.
  • This approach opens new avenues for investigating cyclic and non-cyclic enzymatic reactions.
  • Enables detailed analysis of substrate-triggered biological processes at near-atomic resolution.