Protein crystals IR laser ablated from aqueous solution at high speed retain their diffractive properties: applications in high-speed serial crystallography
作者： Henrike M. Müller-Werkmeister , Emil F. Pai , Wesley D. Robertson , R. J. Dwayne Miller , Eike C. Schulz
DOI: 10.1107/S1600576717014479
关键词:
摘要: In order to utilize the high repetition rates now available at X-ray free-electron laser sources for serial crystallography, methods must be developed softly deliver large numbers of individual microcrystals and speeds. Picosecond infrared (PIRL) pulses, operating under desorption by impulsive vibrational excitation (DIVE) conditions, selectively excite OH stretch water directly propel excited volume speed with minimized heating effects, nucleation formation or cavitation-induced shock waves, leaving analytes intact undamaged. The soft nature laser-based sampling flexibility provided technique make PIRL system an interesting crystal delivery approach crystallography. This paper demonstrates that protein crystals extracted from aqueous buffer solution via PIRL-DIVE ablation retain their diffractive properties can usefully exploited structure determination synchrotron sources. remaining steps implement technology high-speed femtosecond such as single-crystal localization, synchronization, are described. proof-of-principle experiment viability a new without need liquid-jet injectors fixed-target mounting solutions.
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