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Updated: Jan 24, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
Published on: November 21, 2010
A novel handling-free method of mounting single protein crystals for synchrotron structure analyses at room
Yoshihisa Suzuki1, Kumi Torii2, Koji Inaka3
1Graduate School of Technology, Industrial and Social Sciences, Tokushima University, 2-1 Minamijosanjima, Tokushima 770-8506, Japan.
Abstract:
We have developed a handling-free mounting method for X-ray crystallography of protein crystals at room temperatures-the glass capillary method. In this method, crystals were nucleated and grown on the capillary walls, and then, growth solutions were gently removed. The procedures for collecting data on the crystals were conducted by simply setting the capillary on the goniometer of a synchrotron beamline without touching the crystals. Crystal quality was characterized using mosaicity, resolution at I/σ(I) = 2, I/σ(I) at resolution = 2.0 Å, Rmerge, and completeness. Wilson plots were also used to characterize the quality of crystals. In particular, all samples showed very low mosaicity; the handling-free method successfully retained their low mosaicity and effectively maintained the crystal quality.
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