5FEK

Hen egg lysozyme at room temperature solved from 3600 diffraction images acquired by ultrasonic acoustic levitation method and processed by CrystFEL

Summary for 5FEK

• Entry DOI: 10.2210/pdb5fek/pdb
• Descriptor: Lysozyme C, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: Gallus gallus (Chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14448.05

Authors

Tsujino, S.,Tomizaki, T. (deposition date: 2015-12-17, release date: 2016-05-25, Last modification date: 2024-10-23)

Primary citation

Tsujino, S.,Tomizaki, T.
Ultrasonic acoustic levitation for fast frame rate X-ray protein crystallography at room temperature.
Sci Rep, 6:25558-25558, 2016

PubMed Abstract: Increasing the data acquisition rate of X-ray diffraction images for macromolecular crystals at room temperature at synchrotrons has the potential to significantly accelerate both structural analysis of biomolecules and structure-based drug developments. Using lysozyme model crystals, we demonstrated the rapid acquisition of X-ray diffraction datasets by combining a high frame rate pixel array detector with ultrasonic acoustic levitation of protein crystals in liquid droplets. The rapid spinning of the crystal within a levitating droplet ensured an efficient sampling of the reciprocal space. The datasets were processed with a program suite developed for serial femtosecond crystallography (SFX). The structure, which was solved by molecular replacement, was found to be identical to the structure obtained by the conventional oscillation method for up to a 1.8-Å resolution limit. In particular, the absence of protein crystal damage resulting from the acoustic levitation was carefully established. These results represent a key step towards a fully automated sample handling and measurement pipeline, which has promising prospects for a high acquisition rate and high sample efficiency for room temperature X-ray crystallography.

PubMed: 27150272
DOI: 10.1038/srep25558

Experimental method

X-RAY DIFFRACTION (1.8 Å)