Surface treatment by oxidizing the plates can alter the response of protein crystallization

Guo, Yang; Liu, Yong-Ming; Yin, Da‐Chuan; He, Jinguang; Zhang, Chenyan; Cao, Hui‐Ling; Hou, Hai; Wei, Ma; Guo, Weihong; Shi, Jian-Yu; Cui, Chao; Wang, Zhe; Shang, Peng

doi:10.1107/s1600576713030999

Cited by 8 publications

(3 citation statements)

References 43 publications

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“…The increase in the crystallisation success rate might be attributable to the characteristics of the SDB microspheres. In the literature, we find a number of extensive studies concerning the effect of heterogeneous nucleants on protein nucleation 12 21 22 23 24 25 26 27 28 29 30 31 32 33 34 . Many heterogeneous nucleants (such as mineral substrates, silicon substrates, TiO 2 , SiO 2 , and polystyrene) are reported to promote the nucleation of protein crystals by lowering the energy barrier for nucleation.…”

Section: Discussionmentioning

confidence: 99%

“…Nevertheless, this method cannot be applied to proteins for which the solubility is not affected by temperature changes; moreover, only in situ lightscattering 16 17 can provide information about nucleation in crystallisation droplets, requiring the use of appropriate DLS hardware. In addition to this method, other approaches, such as seeding 18 19 20 or heterogeneous nucleation 12 21 22 23 24 25 26 27 28 29 30 31 32 33 34 , can also be useful for identifying conditions that are suitable for the growth of high-quality protein crystals.…”

mentioning

confidence: 99%

“…As an alternative, heterogeneous nucleation 12 21 22 23 24 25 26 27 28 29 30 31 32 33 34 has been proposed. In particular, Chayen et al 12 have reported the best results regarding heterogeneous nucleation to date using two chemically different materials that possessed broad pore-size distributions 12 .…”

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confidence: 99%

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Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality

Guo

Sun

Oberthüer

et al. 2014

Sci Rep

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High-quality protein crystals of suitable size are an important prerequisite for applying X-ray crystallography to determine the 3-dimensional structure of proteins. However, it is often difficult to obtain protein crystals of appropriate size and quality because nucleation and growth processes can be unsuccessful. Here, we show that by adsorbing proteins onto porous polystyrene-divinylbenzene microspheres (SDB) floating on the surface of the crystallisation solution, a localised high supersaturation region at the surface of the microspheres and a low supersaturation region below the microspheres can coexist in a single solution. The crystals will easily nucleate in the region of high supersaturation, but when they grow to a certain size, they will sediment to the region of low supersaturation and continue to grow. In this way, the probability of crystallisation and crystal quality can be simultaneously increased in a single solution without changing other crystallisation parameters.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality

Guo

Sun

Oberthüer

et al. 2014

Sci Rep

Self Cite

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Understanding Biomolecular Crystallization on Amyloid‐Like Superhydrophobic Biointerface

Gao

Tao

et al. 2018

Adv Materials Inter

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biohybrids. [6] With respect to the crystallization, a protein-based biopolymer substrate is typically utilized in nature to develop excellent biomineralization system. [7] Vice versa, the utilization of mineral substrates, [8] chemically modified mica, [9] gel, [10] silanized polystyrene wells, [11] lipid layers, [12] polymeric film surfaces [13] as well as porous media, [14] etc. have contributed a lot to protein crystallization. Some conjectures have been made from these studies, typically including concentration effect-induced change of supersaturation extent near a surface, [15] adsorption of solutes on a surface, [16] specific interaction between solutes and chemically modified surfaces, [17] the presence of surface microtopography, and spatial characteristics to guide nucleation and crystalline lattice. [18] However, despite immense progress, understanding the crystallization mechanism of proteins and peptides on solid surface remains elusive, and more fundamental clues to reveal this process should be discovered. In this regard, a superhydrophobic surface would be an ideal platform for the crystallization design, since such an interface exhibits great feasibility to concentrate solutes in the sessile droplet [19] and this simplified model induces efficient crystallization of salts, [20] colloidal assembly [21] as well as detection enhancement. [22] Such a platform actually has found a wide range of important applications in current medicine and biotechnology, [23] such as protein adsorption, [24a] drug release, [24b,c] cellular interaction, [24d] and so on. [24e]

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Effect of real-world sounds on protein crystallization

Zhang

Liu

Tian

et al. 2018

International Journal of Biological Macromolecules

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Surface treatment by oxidizing the plates can alter the response of protein crystallization

Cited by 8 publications

References 43 publications

Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality

Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality

Understanding Biomolecular Crystallization on Amyloid‐Like Superhydrophobic Biointerface

Effect of real-world sounds on protein crystallization

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