Room-temperature crystallography using a microfluidic protein crystal array device and its application to protein-ligand complex structure analysis.

Chemical Science
Masatoshi MaekiManabu Tokeshi

Abstract

Room-temperature (RT) protein crystallography provides significant information to elucidate protein function under physiological conditions. In particular, contrary to typical binding assays, X-ray crystal structure analysis of a protein-ligand complex can determine the three-dimensional (3D) configuration of its binding site. This allows the development of effective drugs by structure-based and fragment-based (FBDD) drug design. However, RT crystallography and RT crystallography-based protein-ligand complex analyses require the preparation and measurement of numerous crystals to avoid the X-ray radiation damage. Thus, for the application of RT crystallography to protein-ligand complex analysis, the simultaneous preparation of protein-ligand complex crystals and sequential X-ray diffraction measurement remain challenging. Here, we report an RT crystallography technique using a microfluidic protein crystal array device for protein-ligand complex structure analysis. We demonstrate the microfluidic sorting of protein crystals into microwells without any complicated procedures and apparatus, whereby the sorted protein crystals are fixed into microwells and sequentially measured to collect X-ray diffraction data. This is followed by...Continue Reading

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Citations

May 6, 2021·Acta Crystallographica. Section D, Structural Biology·Gabrielle IllavaRobert E Thorne

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Methods Mentioned

BETA
protein crystallography
X-ray
protein
protein crystal array
Partial diffraction
protein crystal sorting
in situ crystallography

Software Mentioned

KAMO
XSCALE
phenix
Beamline Scheduling Software ( BSS )
. phaser
RADDOSE
COOT

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