Optimization of the critical nuclear size for protein crystallization: a note

2000 ◽  
Vol 56 (1) ◽  
pp. 106-108 ◽  
Author(s):  
Emmanuel Saridakis
Keyword(s):  
Local Minimum ◽  
Critical Radius ◽  
Protein Crystallization ◽  
Nuclear Size ◽  
X Ray Diffraction ◽  
X Ray

It was observed that for some proteins the best crystals for X-ray diffraction have been obtained at supersaturation ratios of ca 2.5–3 (in experiments without seeding). It was then noticed that under certain conditions specific to the protein such values are close to a local minimum of the critical radius for nucleation. A relation between the two observations is proposed.

Structural and superconducting properties of melt-grown Y–Ba–Cu–O superconductors

1996 ◽  
Vol 11 (10) ◽  
pp. 2406-2415 ◽  
Author(s):  
R. Gopalan ◽  
T. Rajasekharan ◽  
T. Roy ◽  
G. Rangarajan ◽  
V. Ganesan ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Strain Field ◽  
Crack Width ◽  
Growth Process ◽  
Critical Radius ◽  
Radius Of Curvature ◽  
Superconducting Properties ◽  
X Ray Diffraction ◽  
X Ray ◽  
Transmission Electron

YBa2Cu3O7 (123) samples with varying Y2BaCuO5 (211) concentrations (0 mol%, 20 mol%, 28 mol%, and 50 mol%) were synthesized by the melt-growth process. Microstructural characterizations were done using x-ray diffraction (XRD), optical microscopy, scanning electron microscopy, and transmission electron microscopy (TEM). It was found that 123 platelet width, crack width between the platelets, and 211 particle size decreased systematically with increasing 211 concentration. TEM study showed that there is a critical radius of curvature (rc ≤ 0.2 μm-0.3 μm) of the 123/211 interface where defects/contrasts of strain field start to appear, and these defects are believed to be responsible for pinning the magnetic flux. Microhardness measurements showed that Vickers hardness (VHN) increases with increasing 211 content. Critical current density (Jc) values obtained from magnetization measurements using a SQUID magnetometer were found to increase in melt-grown samples by the addition of 211 content.

Polysaccharides as Precipitants in Protein Crystallization for X-Ray Diffraction Studies

2011 ◽  
Vol 11 (4) ◽  
pp. 1152-1158 ◽  
Author(s):  
Laura Vepsäläinen ◽  
Katja Palmunen ◽  
Sinikka Uotila ◽  
Kalevi Visuri ◽  
Juha Rouvinen ◽  
...  
Keyword(s):  
Protein Crystallization ◽  
X Ray Diffraction ◽  
X Ray

scholarly journals In-plate protein crystallization,in situligand soaking and X-ray diffraction

2011 ◽  
Vol 67 (9) ◽  
pp. 747-755 ◽  
Author(s):  
Albane le Maire ◽  
Muriel Gelin ◽  
Sylvie Pochet ◽  
François Hoh ◽  
Michel Pirocchi ◽  
...  
Keyword(s):  
Protein Crystallization ◽  
X Ray Diffraction ◽  
X Ray

Estimation of The Critical Radius for The Nucleation of the C54 Phase in C49 TiSi2: Role of The Difference in Density

1999 ◽  
Vol 580 ◽  
Author(s):  
D.B. Migas ◽  
M. Iannuzzi ◽  
Leo Miglio ◽  
F. La Via ◽  
M.G. Grimaldi
Keyword(s):  
Ab Initio ◽  
Elastic Strain ◽  
Critical Radius ◽  
Lattice Parameters ◽  
X Ray Diffraction ◽  
X Ray ◽  
The Difference ◽  
Two Phases ◽  
The One

AbstractWe discuss the rather scattered measurements of the lattice parameters for C49 TiSi2, which are reported in literature, along with new and accurate X-ray diffraction measurements and ab-initio calculations. Both agree in indicating that the density of the metastable C49 structure cannot be much smaller than the one for the polymorphic C54 phase, as it is commonly reported. We conclude by demonstrating that only in the case of such a smaller difference in density between the two phases, the elastic strain contribution to the nucleation energy of the C54 structure in the C49 matrix can be neglected. The estimation of the critical radius strongly depends on this issue.

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.

On increasing protein-crystallization throughput for X-ray diffraction studies

2005 ◽  
Vol 61 (2) ◽  
pp. 123-129 ◽  
Author(s):  
Ashit K. Shah ◽  
Zhi-Jie Liu ◽  
Patrick D. Stewart ◽  
Florian D. Schubot ◽  
John P. Rose ◽  
...  
Keyword(s):  
Protein Crystallization ◽  
X Ray Diffraction ◽  
X Ray

scholarly journals Application of protein engineering to enhance crystallizability and improve crystal properties

2010 ◽  
Vol 66 (5) ◽  
pp. 604-615 ◽  
Author(s):  
Zygmunt S. Derewenda
Keyword(s):  
Protein Engineering ◽  
Model Building ◽  
Protein Crystallization ◽  
X Ray Diffraction ◽  
X Ray ◽  
Rate Limiting Step ◽  
Technological Advances ◽  
Radiation Sources ◽  
Crystal Properties ◽  
Automated Model Building

Until recently, protein crystallization has mostly been regarded as a stochastic event over which the investigator has little or no control. With the dramatic technological advances in synchrotron-radiation sources and detectors and the equally impressive progress in crystallographic software, including automated model building and validation, crystallization has increasingly become the rate-limiting step in X-ray diffraction studies of macromolecules. However, with the advent of recombinant methods it has also become possible to engineer target proteins and their complexes for higher propensity to form crystals with desirable X-ray diffraction qualities. As most proteins that are under investigation today are obtained by heterologous overexpression, these techniques hold the promise of becoming routine tools with the potential to transform classical crystallization screening into a more rational high-success-rate approach. This article presents an overview of protein-engineering methods designed to enhance crystallizability and discusses a number of examples of their successful application.

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