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An investigation on the effect of surface roughness of crystallization plate on protein crystallization

Published on Jun 1, 2017in Journal of Crystal Growth1.573
· DOI :10.1016/j.jcrysgro.2016.10.007
Hai Hou4
Estimated H-index: 4
(NPU: Northwestern Polytechnical University),
Bo Wang3
Estimated H-index: 3
(NPU: Northwestern Polytechnical University)
+ 4 AuthorsDa-Chuan Yin19
Estimated H-index: 19
(NPU: Northwestern Polytechnical University)
Abstract
Abstract Surface treatment by oxidizing the crystallization plates can significantly promote protein crystallization and requires no change to routine screening protocols; therefore, it is potentially useful for practical protein crystallization screening. However, experiments have shown that the amount of oxidants and the treatment process need to be optimized to achieve effective results. Searching for the suitable amount of oxidants, temperature and processing time for surface treatment of the plate will increase the workload and decrease the efficiency of the screening process. To solve this problem, a series of trials to determine suitable surface treatment conditions were conducted. Based on these experiments, not only was the most suitable processing condition for the optimal protein crystallization screening hits discovered but also the relationship between the treatment process and the protein crystallization screening hits was explored. With these results, the surface treatment of protein crystallization plates became easier and more effective, allowing the oxidizing surface treatment method to be applied on plates for use in routine protein crystallization screening.
  • References (16)
  • Citations (1)
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References16
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#1Yun-Zhu Guo (NPU: Northwestern Polytechnical University)H-Index: 9
#2Yong-Ming Liu (NPU: Northwestern Polytechnical University)H-Index: 7
Last. Peng Shang (NPU: Northwestern Polytechnical University)H-Index: 21
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This report describes the modification of crystallization plates by simply oxidizing the surface of the protein wells. The oxidized crystallization plates were tested in standard protein crystallization screening and reproducibility studies. The results showed that the protein wells of the treated plates were smoother and more optically transparent than those of the untreated plates, and more importantly, protein crystallization was significantly promoted after the oxidation treatment. Because t...
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#1F. Kertis (Johns Hopkins University)H-Index: 2
#2Sahir Khurshid (Imperial College London)H-Index: 10
Last. Jonah Erlebacher (Johns Hopkins University)H-Index: 38
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We present a theory and experiments that help clarify the origin of the effectiveness of nanoporous substrates in the heterogeneous nucleation of protein crystals. The central idea tested here is that when a substrate (or “nucleant”) possesses pores of the order of the hydrodynamical radius of a protein, then the entropic penalty associated with nucleating a protein crystal on that surface may be alleviated. Model experiments using lysozyme and nanoporous gold (NPG) substrates suggest that there...
21 CitationsSource
#1Victor M. Bolanos-Garcia (University of Cambridge)H-Index: 24
#2Naomi E. Chayen (Imperial College London)H-Index: 34
Novel strategies and techniques that are based on conventional crystallization methods for crystallizing proteins are described and discussed. New directions for rendering proteins and protein complexes to become more amenable to crystallization are also presented.
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#1Johanna KallioH-Index: 13
#2Nina HakulinenH-Index: 17
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Background Protein crystallization is a slow process of trial and error and limits the amount of solved protein structures. Search of a universal heterogeneous nucleant is an effort to facilitate crystallizability of proteins.
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