Improving Protein Crystal Quality via Mechanical Vibration

Lu, Qi; Zhang, Bin; Liang, Tao; Xu, Lu; Chen, Da; Zhu, Jing; Yin, Da‐Chuan

doi:10.1021/acs.cgd.6b00227

Cited by 8 publications

(3 citation statements)

References 57 publications

(78 reference statements)

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“…Since protein crystallization is highly sensitive to environmental factors (sound, light, electric and magnetic fields, gravitational field, heat, mechanical vibration, and so on), − investigation of the effects of the environments on protein crystallization is essential for good control of the crystallization process to produce desirable results. Audible sound has been shown to be an environmental factor that affects the process of protein crystallization .…”

Section: Introductionsupporting

confidence: 93%

Protein Crystallization Irradiated by Audible Sound: The Effect of Varying Sound Frequency

Zhang

Liu

Wang

et al. 2018

Crystal Growth & Design

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Protein crystallization is a process that is very sensitive to the physical environment. Audible sound is an environmental characteristic that can significantly affect the crystallization process. Previously, it was found that the crystallization result is frequency dependent, that is, the crystallization of protein under different sound frequencies yields different results. Here, we further investigate the effect of varying frequency (or a frequency program) on protein crystallization. Twelve different frequency programs and six proteins were used to test the effect of varying sound frequency on protein crystallization. The results showed that varying the audible sound frequency from high to low exhibited the most significant improvement in protein crystallization. Varying frequency linearly from 15 000 to 100 Hz in 12 h best promoted crystallization, with the average number of crystallization hits 36.5% higher than in the control. Crystal quality was improved with sound irradiation using STW2 program. Our study showed that varying the sound frequency has positive effects on facilitating protein crystallization and purposely optimizing sound frequency programs may be helpful for obtaining protein crystals.

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Section: Introductionsupporting

confidence: 93%

Protein Crystallization Irradiated by Audible Sound: The Effect of Varying Sound Frequency

Zhang

Liu

Wang

et al. 2018

Crystal Growth & Design

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“…In this method, seed crystals are mainly inoculated into the pre-balanced protein crystal solution in metastable state, and the nucleation process is shortened by introducing foreign seed crystals to induce protein nucleation at low supersaturation, so as to obtain a highly ordered protein structure. To improve the quality of protein crystals by using tools such as electric fields [4,5], magnetic fields, ultrasound waves, light, mechanical vibration [6], microgravity [7,8], and nucleants [9], has always been studied. The addition of nucleants is one of the most commonly used methods for improving the quality of protein crystals.…”

Section: Introductionmentioning

confidence: 99%

Comparison of the Quality of Protein Crystals Grown by CLPC Seeds Method

Yan

Liu

et al. 2019

Crystals

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We present a systematic quality comparison of protein crystals obtained with and without cross-linked protein crystal (CLPC) seeds. Four proteins were used to conduct the experiments, and the results showed that crystals obtained in the presence of CLPC seeds exhibited a better morphology. In addition, the X-ray diffraction data showed that the CLPC seeds method is a powerful tool to obtain high-quality protein crystals. Therefore, we recommend the use of CLPC seeds in preparing high-quality diffracting protein crystals.

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“…Protein crystallization is a highly useful process in that it can not only prepare protein crystals for the structural determination of protein molecules (one of the prevailing methods to obtain high resolution molecular structures of proteins) but also provide highly purified proteins for various purposes including biopharmaceuticals, the food industry, chemical agents, catalysis, and environmental engineering . Since the crystallization of a protein is frequently difficult, the development of methods to enhance protein crystallization is always important. − …”

Section: Introductionmentioning

confidence: 99%

Utilization of Cyclodextrins and Its Derivative Particles as Nucleants for Protein Crystallization

Yang

Zhang

Wang

et al. 2017

Crystal Growth & Design

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Finding new nucleants to promote protein crystallization is an important task, especially for purposes other than structural determination. Here, we investigated cyclodextrins and its derivative particles, as potential nucleants for protein crystallization. β-Cyclodextrin (β-CD) and its derivatives (including p-toluenesulfonyl-β-cyclodextrin (PTCD), polymer-β-cyclodextrin (PCD), mono-(6-(1,6-hexamethylenediamine)-6-deoxy)-β-cyclodextrin (MHCD) and mercapto-β-cyclodextrin (MCD)) were used as nucleants. The experimental results confirmed that β-CD and its derivatives showed significantly positive effects, promoting protein crystallization and improving crystal quality. A larger number of protein molecules (including lysozyme, catalase, subtilisin A VIII, concanavalin A VI, α-chymotrypsinogen, proteinase K, cellulase, papain, glucose isomerase, hemoglobin, and ribonuclease A XII) attached to the particles usually corresponded to a higher crystallization success rate. More detailed analysis showed that cyclodextrins exhibited the best performance when the overall charge of protein in solution was the opposite to zeta potential of the cyclodextrins particle. Our results showed that cyclodextrins can be useful as nucleants due to the ease of modifying them to suit the crystallization of different proteins, and they can be explored for use in the mass purification of proteins for the biopharmaceutical industry. Furthermore, the phenomenon discovered in this study pointed toward a way to find new nucleants based on the overall charge of proteins in a solution: the nucleants should preferably be the opposite between the overall charge of target protein and the zeta potential of the cyclodextrin particle.

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Improving Protein Crystal Quality via Mechanical Vibration

Cited by 8 publications

References 57 publications

Protein Crystallization Irradiated by Audible Sound: The Effect of Varying Sound Frequency

Protein Crystallization Irradiated by Audible Sound: The Effect of Varying Sound Frequency

Comparison of the Quality of Protein Crystals Grown by CLPC Seeds Method

Utilization of Cyclodextrins and Its Derivative Particles as Nucleants for Protein Crystallization

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