Titelbild: A Droplet-Based, Composite PDMS/Glass Capillary Microfluidic System for Evaluating Protein Crystallization Conditions by Microbatch and Vapor-Diffusion Methods with On-Chip X-Ray Diffraction (Angew. Chem. 19/2004)

2004 ◽  
Vol 116 (19) ◽  
pp. 2509-2509 ◽  
Author(s):  
Bo Zheng ◽  
Joshua D. Tice ◽  
L. Spencer Roach ◽  
Rustem F. Ismagilov
Keyword(s):  
Protein Crystallization ◽  
Microfluidic System ◽  
X Ray Diffraction ◽  
Glass Capillary ◽  
Vapor Diffusion ◽  
X Ray ◽  
Crystallization Conditions ◽  
On Chip

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.

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.

scholarly journals Nanovolume optimization of protein crystal growth using the microcapillary protein crystallization system

2010 ◽  
Vol 43 (5) ◽  
pp. 1078-1083 ◽  
Author(s):  
Cory J. Gerdts ◽  
Glenn L. Stahl ◽  
Alberto Napuli ◽  
Bart Staker ◽  
Jan Abendroth ◽  
...  
Keyword(s):  
Protein Crystallization ◽  
Protein Structures ◽  
Protein Crystal ◽  
X Ray Diffraction ◽  
Vapor Diffusion ◽  
X Ray ◽  
Gradient Optimization ◽  
Crystallization System ◽  
Initial Crystal ◽  
Novel Protein

The Microcapillary Protein Crystallization System (MPCS) is a microfluidic, plug-based crystallization technology that generates X-ray diffraction-ready protein crystals in nanolitre volumes. In this study, 28 out of 29 (93%) proteins crystallized by traditional vapor diffusion experiments were successfully crystallized by chemical gradient optimization experiments using the MPCS technology. In total, 90 out of 120 (75%) protein/precipitant combinations leading to initial crystal hits from vapor diffusion experiments were successfully crystallized using MPCS technology. Many of the resulting crystals produced high-quality X-ray diffraction data, and six novel protein structures that were derived from crystals harvested from MPCS CrystalCards are reported.

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.

Screening and optimization of protein crystallization conditions through gradual evaporation using a novel crystallization platform

2005 ◽  
Vol 38 (6) ◽  
pp. 988-995 ◽  
Author(s):  
Sameer Talreja ◽  
David Y. Kim ◽  
Amir Y. Mirarefi ◽  
Charles F. Zukoski ◽  
Paul J. A. Kenis
Keyword(s):  
Phase Transition ◽  
High Throughput Screening ◽  
Large Fraction ◽  
Protein Crystallization ◽  
Rapid Screening ◽  
Successful Implementation ◽  
X Ray Diffraction ◽  
X Ray ◽  
Wide Range ◽  
Crystallization Conditions

High-throughput screening of a wide range of different conditions is typically required to obtain X-ray quality crystals of proteins for structure–function studies. The outcomes of individual experiments,i.e.the formation of gels, precipitates, microcrystals, or crystals, guide the search for and optimization of conditions resulting in X-ray diffraction quality crystals. Unfortunately, the protein will remain soluble in a large fraction of the experiments. In this paper, an evaporation-based crystallization platform is reported in which droplets containing protein and precipitant are gradually concentrated through evaporation of solvent until the solvent is completely evaporated. A phase transition is thus ensured for each individual crystallization compartment; hence the number of experiments and the amount of precious protein needed to identify suitable crystallization conditions is reduced. The evaporation-based method also allows for rapid screening of different rates of supersaturation, a parameter known to be important for optimization of crystal growth and quality. The successful implementation of this evaporation-based crystallization platform for identification and especially optimization of crystallization conditions is demonstrated using the model proteins of lysozyme and thaumatin.

Evaluation of Freezing Methods by Low Temperature X-Ray Diffraction

1977 ◽  
Vol 35 ◽  
pp. 330-333
Author(s):  
T. Gulik-Krzywicki ◽  
M.J. Costello
Keyword(s):  
Biological Materials ◽  
Molecular Organization ◽  
X Ray Diffraction ◽  
Glass Capillary ◽  
X Ray ◽  
Rate Dependent ◽  
Before And After ◽  
Freeze Etching ◽  
Diffraction Patterns ◽  
Set Up

Freeze-etching electron microscopy is currently one of the best methods for studying molecular organization of biological materials. Its application, however, is still limited by our imprecise knowledge about the perturbations of the original organization which may occur during quenching and fracturing of the samples and during the replication of fractured surfaces. Although it is well known that the preservation of the molecular organization of biological materials is critically dependent on the rate of freezing of the samples, little information is presently available concerning the nature and the extent of freezing-rate dependent perturbations of the original organizations. In order to obtain this information, we have developed a method based on the comparison of x-ray diffraction patterns of samples before and after freezing, prior to fracturing and replication.Our experimental set-up is shown in Fig. 1. The sample to be quenched is placed on its holder which is then mounted on a small metal holder (O) fixed on a glass capillary (p), whose position is controlled by a micromanipulator.

Optimization of Structure of Soft Block for Design of Adaptive Polyurethanes

2020 ◽  
Vol 869 ◽  
pp. 273-279
Author(s):  
Marina A. Gorbunova ◽  
Denis V. Anokhin ◽  
Valentina A. Lesnichaya ◽  
Alexander A. Grishchuk ◽  
Elmira R. Badamshina
Keyword(s):  
Mutual Influence ◽  
Glycol Adipate ◽  
Mass Ratio ◽  
X Ray Diffraction ◽  
Scanning Calorimetry ◽  
X Ray ◽  
Crystallization Conditions ◽  
Crystalline Domains ◽  
Kinetics Of

A synthesis of new di-and triblock polyurethane thermoplastic copolymers containing different mass ratio of two crystallizing blocks - poly (1,4-butylene glycol) adipate and poly-ε-caprolactone diols was developed. Using combination of danamometric analysis, IR-spectroscopy, differential scanning calorimetry and X-ray diffraction, the effect of the soft block composition and crystallization conditions on crystal structure and thermal behavior of the obtained polymers have been studied. For the triblock copolymers we have shown a possibility of control the kinetics of material hardening and final mechanical characteristics due to the mutual influence of polydiols during crystallization. In the result, the second crystallizing component allows to control amount, structure and quality of crystalline domains in polyurethanes by variation of crystallization conditions.

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