Channel height dependent protein nucleation and crystal growth in microfluidic devices

Lounaci, M.; Chen, Yong; Rigolet, Pascal

doi:10.1016/j.mee.2009.11.154

Cited by 8 publications

(6 citation statements)

References 14 publications

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“…107 Lounaci et al have shown that crystallization of lysozyme in microcrystallizers is dependent on the channel height (18− 150μm): deeper channels favor nucleation, shallow channels favor growth. 110 They propose a decoupling strategy based on sections of different channel heights rather than different temperatures. 110 II.2.…”

mentioning

confidence: 99%

A Review of Experimental Methods for Nucleation Rate Determination in Large-Volume Batch and Microfluidic Crystallization

Devos

Gerven

Kuhn

2021

Crystal Growth & Design

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Experimental nucleation rate determination for crystallization in solution has been acknowledged as an important topic for a long time, as it improves the design and control of industrial crystallization processes, and offers insights into the mechanisms of nucleation. Characterization of nucleation rates in large volume batch crystallizers has been widely studied in the past, which has led to the development of a variety of models linking the nucleation rate to the metastable zone width and induction time. These methods remain important due to their role in industrial crystallization. More recently, the use of microfluidic platforms has resulted in the development of methods to obtain nucleation rates based on the stochastic nature of nucleation. This has opened new pathways for understanding nucleation on a molecular level. This review presents a critical overview of nucleation rate determination methods: large volume batch crystallizer models (Part I), and microfluidic and microvial models (Part II) are presented in terms of equations, advantages and limitations. Published experimental nucleation rate values are summarized (SI). A critical discussion of experimental nucleation rate determination is given (Part III). The objective of the review is to be a starting point for researchers attempting to experimentally characterize nucleation behavior.

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mentioning

confidence: 99%

A Review of Experimental Methods for Nucleation Rate Determination in Large-Volume Batch and Microfluidic Crystallization

Devos

Gerven

Kuhn

2021

Crystal Growth & Design

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“…Such substrates are designated as universal nucleant [11][12][13][14][15], the large standard deviation in feature size of which has been shown to diminish the energy barrier for nucleation [11]. Not only the size of surface features, but also their shape has been found to influence crystal nucleation [16][17][18]. Nanopores imprinted on polymeric surfaces have been shown to impose angle specific heterogeneity which leads to specific polymorphs of a compound [16].…”

Section: Introductionmentioning

confidence: 99%

Precipitant-Free Crystallization of Protein Molecules Induced by Incision on Substrate

2017

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Nucleation of protein crystals has been shown to be facilitated by substrates decorated with both nano-to micro-scale hierarchical undulations and spatially varying surface potential. In fact, on such surfaces, several proteins were found to crystallize without having to use any precipitant in contrast to all other homogeneous and heterogeneous systems in which precipitant is an essential ingredient for nucleation. While these surfaces were so patterned whole through the area that was brought in contact with the protein solution, it was not clear exactly to what extent the surfaces were required to be patterned to trigger nucleation without use of any precipitant. Here we show that a simple incision may be enough on an otherwise smooth surface for this purpose. In particular, the substrate used here is a smooth silicone film with its surface plasma oxidized to create a thin crust of silica. An incision is then generated on this surface using a sharp razor blade. The silica crust being brittle leads to random nano-microscopic undulations at the vicinity of the incision. These undulations along with surface charge can induce protein crystal nucleation without precipitant.

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“…Reports indicate that the mechanism of protein crystallization is affected by the depth of the microchannel 15 and the nature of the solid surface. [16][17][18][19] In the previous report, we demonstrated that the volume and shape of the nanodroplet influence the protein crystallization behaviour, i.e.…”

Section: Introductionmentioning

confidence: 99%

Three-dimensional Raman spectroscopic imaging of protein crystals deposited on a nanodroplet

Nitahara

Maeki

Yamaguchi

et al. 2012

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Confocal Raman spectroscopic imaging has been used to find the location of protein crystals deposited in a nanodroplet. The depth of the protein crystal has been clearly identified by comparing the three-dimensional Raman spectroscopic images of the protein with those of water. Additionally, the low concentration region around a growing protein crystal in the nanodroplet was visualized using two-dimensional Raman spectroscopic imaging.

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Channel height dependent protein nucleation and crystal growth in microfluidic devices

Cited by 8 publications

References 14 publications

A Review of Experimental Methods for Nucleation Rate Determination in Large-Volume Batch and Microfluidic Crystallization

A Review of Experimental Methods for Nucleation Rate Determination in Large-Volume Batch and Microfluidic Crystallization

Precipitant-Free Crystallization of Protein Molecules Induced by Incision on Substrate

Three-dimensional Raman spectroscopic imaging of protein crystals deposited on a nanodroplet

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