Imperial College London
Dr Emmanuel Saridakis

DrEmmanuelSaridakis

Faculty of Medicine, Department of Metabolism, Digestion and Reproduction

Honorary Senior Research Fellow
 
 
 
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Contact

 

e.saridakis

 
 
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Location

 

OP14Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Nanev:2017:10.1038/srep35821,
author = {Nanev, CN and Saridakis, E and Chayen, N},
doi = {10.1038/srep35821},
journal = {Scientific Reports},
title = {Protein crystal nucleation in pores},
url = {http://dx.doi.org/10.1038/srep35821},
volume = {7},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The most powerful method for protein structure determination is X-ray crystallography which relies on the availability of high quality crystals. Obtaining protein crystals is a major bottleneck, and inducing their nucleation is of crucial importance in this field. An effective method to form crystals is to introduce nucleation-inducing heterologous materials into the crystallization solution. Porous materials are exceptionally effective at inducing nucleation. It is shown here that a combined diffusion-adsorption effect can increase protein concentration inside pores, which enables crystal nucleation even under conditions where heterogeneous nucleation on flat surfaces is absent. Provided the pore is sufficiently narrow, protein molecules approach its walls and adsorb more frequently than they can escape. The decrease in the nucleation energy barrier is calculated, exhibiting its quantitative dependence on the confinement space and the energy of interaction with the pore walls. These results provide a detailed explanation of the effectiveness of porous materials for nucleation of protein crystals, and will be useful for optimal design of such materials.
AU  - Nanev,CN
AU  - Saridakis,E
AU  - Chayen,N
DO  - 10.1038/srep35821
PY  - 2017///
SN  - 2045-2322
TI  - Protein crystal nucleation in pores
T2  - Scientific Reports
UR  - http://dx.doi.org/10.1038/srep35821
UR  - http://hdl.handle.net/10044/1/43685
VL  - 7
ER  -
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