scholarly journals A microfluidic device for both on-chip dialysis protein crystallization and in situ X-ray diffraction

Lab on a Chip ◽  
2020 ◽  
Vol 20 (2) ◽  
pp. 296-310 ◽  
Author(s):  
Niels Junius ◽  
Sofia Jaho ◽  
Yoann Sallaz-Damaz ◽  
Franck Borel ◽  
Jean-Baptiste Salmon ◽  
...  
Keyword(s):  
Microfluidic Device ◽  
Microfluidic Chip ◽  
Protein Crystallization ◽  
X Ray Diffraction ◽  
X Ray ◽  
Dialysis Method ◽  
On Chip

This paper reports a versatile microfluidic chip developed for on-chip crystallization of proteins through the dialysis method and in situ X-ray diffraction experiments.

scholarly journals Room-temperature serial crystallography using a kinetically optimized microfluidic device for protein crystallization and on-chip X-ray diffraction. Corrigendum

IUCrJ ◽  
2015 ◽  
Vol 2 (5) ◽  
pp. 601-601 ◽  
Author(s):  
Michael Heymann ◽  
Achini Opathalage ◽  
Jennifer L. Wierman ◽  
Sathish Akella ◽  
Doletha M. E. Szebenyi ◽  
...  
Keyword(s):  
Microfluidic Device ◽  
Room Temperature ◽  
Protein Crystallization ◽  
X Ray Diffraction ◽  
X Ray ◽  
Serial Crystallography ◽  
On Chip

The name of one of the authors in the article by Heymannet al.[(2014),IUCrJ,1, 349–360] is corrected.

Combining `dry' co-crystallization andin situdiffraction to facilitate ligand screening by X-ray crystallography

2015 ◽  
Vol 71 (8) ◽  
pp. 1777-1787 ◽  
Author(s):  
Muriel Gelin ◽  
Vanessa Delfosse ◽  
Frédéric Allemand ◽  
François Hoh ◽  
Yoann Sallaz-Damaz ◽  
...  
Keyword(s):  
Protein Crystallization ◽  
X Ray Diffraction ◽  
X Ray ◽  
X Ray Crystallography ◽  
Ligand Screening ◽  
Alternative Approach ◽  
Manual Handling ◽  
Stock Solutions ◽  
Established Technique

X-ray crystallography is an established technique for ligand screening in fragment-based drug-design projects, but the required manual handling steps – soaking crystals with ligand and the subsequent harvesting – are tedious and limit the throughput of the process. Here, an alternative approach is reported: crystallization plates are pre-coated with potential binders prior to protein crystallization and X-ray diffraction is performed directly `in situ' (or in-plate). Its performance is demonstrated on distinct and relevant therapeutic targets currently being studied for ligand screening by X-ray crystallography using either a bending-magnet beamline or a rotating-anode generator. The possibility of using DMSO stock solutions of the ligands to be coated opens up a route to screening most chemical libraries.

scholarly journals Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies

10.3791/61660 ◽  
2021 ◽  
Author(s):  
Sofia Jaho ◽  
Niels Junius ◽  
Franck Borel ◽  
Yoann Sallaz-Damaz ◽  
Jean-Baptiste Salmon ◽  
...  
Keyword(s):  
X Ray Diffraction ◽  
X Ray ◽  
On Chip

A Method of Cryoprotection for Protein Crystallography by Using a Microfluidic Chip and Its Application for in Situ X-ray Diffraction Measurements

2015 ◽  
Vol 87 (8) ◽  
pp. 4194-4200 ◽  
Author(s):  
Masatoshi Maeki ◽  
Ashtamurthy S. Pawate ◽  
Kenichi Yamashita ◽  
Masahide Kawamoto ◽  
Manabu Tokeshi ◽  
...  
Keyword(s):  
Microfluidic Chip ◽  
Protein Crystallography ◽  
X Ray Diffraction ◽  
X Ray

scholarly journals Room-temperature serial crystallography using a kinetically optimized microfluidic device for protein crystallization and on-chip X-ray diffraction

IUCrJ ◽  
2014 ◽  
Vol 1 (5) ◽  
pp. 349-360 ◽  
Author(s):  
Michael Heymann ◽  
Achini Opthalage ◽  
Jennifer L. Wierman ◽  
Sathish Akella ◽  
Doletha M. E. Szebenyi ◽  
...  
Keyword(s):  
Room Temperature ◽  
Protein Crystallization ◽  
Glucose Isomerase ◽  
Feedback Mechanism ◽  
X Ray Diffraction ◽  
Data Set ◽  
X Ray ◽  
X Ray Crystallography ◽  
Negative Feedback Mechanism ◽  
On Chip

An emulsion-based serial crystallographic technology has been developed, in which nanolitre-sized droplets of protein solution are encapsulated in oil and stabilized by surfactant. Once the first crystal in a drop is nucleated, the small volume generates a negative feedback mechanism that lowers the supersaturation. This mechanism is exploited to produce one crystal per drop. Diffraction data are measured, one crystal at a time, from a series of room-temperature crystals stored on an X-ray semi-transparent microfluidic chip, and a 93% complete data set is obtained by merging single diffraction frames taken from different unoriented crystals. As proof of concept, the structure of glucose isomerase was solved to 2.1 Å, demonstrating the feasibility of high-throughput serial X-ray crystallography using synchrotron radiation.

The Use of Advanced Analytical Techniques for Characterization of the Chemical, Physical, and Crystallographic Nature of a Surface

1973 ◽  
Vol 31 ◽  
pp. 132-133 ◽  
Author(s):  
R. E. Herfert
Keyword(s):  
Surface Characterization ◽  
Analytical Techniques ◽  
X Ray Diffraction ◽  
Depth Of Penetration ◽  
X Ray ◽  
The Past ◽  
Transmission Electron ◽  
Scanning Electron

Studies of the nature of a surface, either metallic or nonmetallic, in the past, have been limited to the instrumentation available for these measurements. In the past, optical microscopy, replica transmission electron microscopy, electron or X-ray diffraction and optical or X-ray spectroscopy have provided the means of surface characterization. Actually, some of these techniques are not purely surface; the depth of penetration may be a few thousands of an inch. Within the last five years, instrumentation has been made available which now makes it practical for use to study the outer few 100A of layers and characterize it completely from a chemical, physical, and crystallographic standpoint. The scanning electron microscope (SEM) provides a means of viewing the surface of a material in situ to magnifications as high as 250,000X.

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