Abstract
We demonstrated the processing of a membrane protein crystal, using a pulsed UV laser soft ablation (PULSA) technique. Irradiation with deep-UV laser pulses at a wavelength of 193 nm successfully processed not only single crystals of the membrane transporter protein AcrB but also nylon loops and cryoprotectants at a cryogenic temperature. Nonprocessed parts of the crystals exhibited no signs of crack or denaturation after the laser exposure. The trimmed crystals were found to be of high resolution for X-ray diffraction data collection. The results described here indicate that PULSA processing is an effective tool for membrane protein crystals, as well as for soluble protein crystals.
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