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Da-chuan Yin - One of the best experts on this subject based on the ideXlab platform.
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Effect of real-world sounds on Protein Crystallization.
International journal of biological macromolecules, 2018Co-Authors: Chen-yan Zhang, Wen-jing Liu, Liu Yue, Xu-hua Tian, Li-xue Yang, Han-jun Jiang, Chong Han, Ke-an Chen, Da-chuan YinAbstract:Protein Crystallization is sensitive to the environment, while audible sound, as a physical and environmental factor during the entire process, is always ignored. We have previously reported that Protein Crystallization can be affected by a computer-generated monotonous sound with fixed frequency and amplitude. However, real-world sounds are not so simple but are complicated by parameters (frequency, amplitude, timbre, etc.) that vary over time. In this work, from three sound categories (music, speech, and environmental sound), we selected 26 different sounds and evaluated their effects on Protein Crystallization. The correlation between the sound parameters and the Crystallization success rate was studied mathematically. The results showed that the real-world sounds, similar to the artificial monotonous sounds, could not only affect Protein Crystallization, but also improve crystal quality. Crystallization was dependent not only on the frequency, amplitude, volume, irradiation time, and overall energy of the sounds but also on their spectral characteristics. Based on these results, we suggest that intentionally applying environmental sound may be a simple and useful tool to promote Protein Crystallization.
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Seeding Protein Crystallization with Cross-Linked Protein Crystals
Crystal Growth & Design, 2018Co-Authors: Er-kai Yan, Chen-yan Zhang, Liu Yue, Feng-zhu Zhao, Xue-zhou Yang, Miao Shi, Liu Yali, Hai Hou, Da-chuan YinAbstract:Protein Crystallization is of great importance because Protein crystals have a number of different important applications, including large-scale purification of Proteins, determination of Protein structure, nanoparticle preparation, and theoretical studies of Crystallization. An approach often used to efficiently crystallize Proteins is the use of nucleants or seeds (small fragments of Protein crystals) that can help increase the probability of Protein Crystallization. Due to the very positive effect that seeding has on Protein Crystallization, seeds are now widely accepted and utilized in practical Protein Crystallization. Here, we show that cross-linked Protein crystals (CLPCs), which retain the crystal structure but are much more stable than non-cross-linked crystals, can also be used as a new type of seed for promoting Protein Crystallization. Seeding with CLPCs has effects on both the reproducibility and screening of Protein crystals and could improve the optical perfection (well-defined facets) of p...
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Utilization of Cyclodextrins and Its Derivative Particles as Nucleants for Protein Crystallization
Crystal Growth & Design, 2017Co-Authors: Xue-zhou Yang, Chen-yan Zhang, Wen-jing Liu, Yun-zhu Guo, Chen Dong, Er-kai Yan, Wang Qianjin, Xi-wang Zheng, Da-chuan YinAbstract: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 cyclode...
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An investigation on the effect of surface roughness of Crystallization plate on Protein Crystallization
Journal of Crystal Growth, 2017Co-Authors: Hai Hou, Meng-ying Wang, Bo Wang, Jinyu Feng, Peng-peng Xie, Da-chuan YinAbstract: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.
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A review on recent advances for nucleants and nucleation in Protein Crystallization
CrystEngComm, 2017Co-Authors: Ren-bin Zhou, Chen-yan Zhang, Hui-ling Cao, Da-chuan YinAbstract:The elucidation of Protein structures by X-ray crystallography remains the most effectual method to provide accurate structural details at atomic resolution for rational drug design and other biotechnological research studies. Also, emerging applications of Protein crystals as ordered nanostructure scaffolds for catalysis, imaging, and drug delivery are attracting much attention. However, the first step of these applications is obtaining high-quality crystals, which is still an obstacle. Successful Crystallization requires two steps: nucleation and crystal growth, while the nucleation is a precondition for harvesting the crystal of interest. So controlling Protein nucleation may be an alternative breakthrough for this bottleneck. It is well known that nucleants can induce Protein Crystallization and improve crystal quality, so investigation on the nucleants that can be universally used for any Protein Crystallization is ongoing. This manuscript reviews the advances that have been achieved using nucleants in Protein Crystallization and it is a suitable reference for practical Crystallization.
Chen-yan Zhang - One of the best experts on this subject based on the ideXlab platform.
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Cyclodextrin and its derivatives enhance Protein Crystallization by grafted on Crystallization plates
Journal of Crystal Growth, 2020Co-Authors: Qian-jin Wang, Gang Zhao, Chen-yan ZhangAbstract:Abstract Protein drugs are attracting increasing attention. Eight of best-selling drugs in worldwide are Proteins. Crystallization is an important Protein purification method; however, it remains a bottleneck step. Heterogeneous nucleate is an effective method of enhancing Protein Crystallization. Cyclodextrin has been widely used in pharmaceutics, and our previous study showed that it is an effective heterogeneous nucleate for enhancing Protein Crystallization, and it may be widely used in purification of Protein drugs. However, cyclodextrin must be added into the Crystallization plate wells by hand, which is labor intensive and is not beneficial to automated Crystallization screening. We grafted β-cyclodextrin (β-CD) and its derivatives (i.e., p-toluenesulfonyl-β-cyclodextrin [PTCD], mono-(6-(1,6-hexamethylenediamine)-6-deoxy)-β-cyclodextrin [MHCD] and mercapto-β-cyclodextrin [MCD]) on Crystallization plates and tested their effects on Protein Crystallization. Protein Crystallization success rate was improved, particularly for the PTCD-grafted group. This is an easy method to facilitate Protein Crystallization and can be widely applied for automatic Crystallization screening.
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Protein Crystallization Irradiated by Audible Sound: The Effect of Varying Sound Frequency
Crystal Growth & Design, 2018Co-Authors: Chen-yan Zhang, Jie Liu, Meng-ying Wang, Wen-jing Liu, Nan Jia, Chang-qing Yang, Ren-bin ZhouAbstract: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. O...
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Effect of real-world sounds on Protein Crystallization.
International journal of biological macromolecules, 2018Co-Authors: Chen-yan Zhang, Wen-jing Liu, Liu Yue, Xu-hua Tian, Li-xue Yang, Han-jun Jiang, Chong Han, Ke-an Chen, Da-chuan YinAbstract:Protein Crystallization is sensitive to the environment, while audible sound, as a physical and environmental factor during the entire process, is always ignored. We have previously reported that Protein Crystallization can be affected by a computer-generated monotonous sound with fixed frequency and amplitude. However, real-world sounds are not so simple but are complicated by parameters (frequency, amplitude, timbre, etc.) that vary over time. In this work, from three sound categories (music, speech, and environmental sound), we selected 26 different sounds and evaluated their effects on Protein Crystallization. The correlation between the sound parameters and the Crystallization success rate was studied mathematically. The results showed that the real-world sounds, similar to the artificial monotonous sounds, could not only affect Protein Crystallization, but also improve crystal quality. Crystallization was dependent not only on the frequency, amplitude, volume, irradiation time, and overall energy of the sounds but also on their spectral characteristics. Based on these results, we suggest that intentionally applying environmental sound may be a simple and useful tool to promote Protein Crystallization.
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Seeding Protein Crystallization with Cross-Linked Protein Crystals
Crystal Growth & Design, 2018Co-Authors: Er-kai Yan, Chen-yan Zhang, Liu Yue, Feng-zhu Zhao, Xue-zhou Yang, Miao Shi, Liu Yali, Hai Hou, Da-chuan YinAbstract:Protein Crystallization is of great importance because Protein crystals have a number of different important applications, including large-scale purification of Proteins, determination of Protein structure, nanoparticle preparation, and theoretical studies of Crystallization. An approach often used to efficiently crystallize Proteins is the use of nucleants or seeds (small fragments of Protein crystals) that can help increase the probability of Protein Crystallization. Due to the very positive effect that seeding has on Protein Crystallization, seeds are now widely accepted and utilized in practical Protein Crystallization. Here, we show that cross-linked Protein crystals (CLPCs), which retain the crystal structure but are much more stable than non-cross-linked crystals, can also be used as a new type of seed for promoting Protein Crystallization. Seeding with CLPCs has effects on both the reproducibility and screening of Protein crystals and could improve the optical perfection (well-defined facets) of p...
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Utilization of Cyclodextrins and Its Derivative Particles as Nucleants for Protein Crystallization
Crystal Growth & Design, 2017Co-Authors: Xue-zhou Yang, Chen-yan Zhang, Wen-jing Liu, Yun-zhu Guo, Chen Dong, Er-kai Yan, Wang Qianjin, Xi-wang Zheng, Da-chuan YinAbstract: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 cyclode...
Xiang-yang Liu - One of the best experts on this subject based on the ideXlab platform.
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From Surface Self-Assembly to Crystallization: Prediction of Protein Crystallization Conditions
The journal of physical chemistry. B, 2006Co-Authors: Yanwei Jia, Xiang-yang LiuAbstract:A new criterion based on surface and volume diffusion kinetics was established to predict Protein Crystallization. Similar to the layer-by-layer crystal growth process of Protein, the kinetics of the two-dimensional self-assembly of Protein at the aqueous solution surface provides a convenient and reliable way to estimate the surface integration and the volume transport during Protein Crystallization. Both the surface and diffusion kinetics were estimated based on the Protein self-assembly at the air/solution interface, which can be obtained by measuring the surface tension. A Crystallization coefficient is found to provide an effective and reliable criterion to predict Protein Crystallization conditions. This criterion has been applied to lysozyme, concanavalin A and BSA Crystallization, and it turns out to be very successful and more reliable than the second virial coefficient criterion.
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Prediction of Protein Crystallization based on interfacial and diffusion kinetics
Applied Physics Letters, 2005Co-Authors: Yanwei Jia, Xiang-yang LiuAbstract:The interfacial kinetics of Protein Crystallization was studied via the kinetics of Protein two-dimensional self-assembly. The competition between the Protein volume transport and surface integration determines whether single crystals or amorphous aggregation will occur. A kinetic coefficient was found to provide an effective and reliable criterion to predict Protein Crystallization conditions. This criterion has been applied to lysozyme, concanavalin A and BSA Crystallization, and it turned out to be very successful and more reliable than the second virial coefficient criterion.
Yong-ming Liu - One of the best experts on this subject based on the ideXlab platform.
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Effect of Audible Sound on Protein Crystallization
Crystal Growth & Design, 2016Co-Authors: Chen-yan Zhang, Yan Wang, Robin Schubert, Liu Yue, Meng-yin Wang, Da Chen, Yun-zhu Guo, Chen Dong, Yong-ming LiuAbstract:The successful Crystallization of Proteins is important because their molecular three-dimensional structures can be obtained through X-ray diffraction when in their crystalline form. Investigation of the Crystallization process is beneficial for this purpose. We have reported that Protein Crystallization is sensitive to audible sound, which is commonly present but is often ignored. Here we investigate the effect of audible sound parameters, especially frequency, on a Protein Crystallization. We show a significant facilitation of Protein Crystallization using 5000 Hz audible sound, possible mechanism was also tried to be clarified. Suitably controlled audible sound can be beneficial for promoting Protein Crystallization. Therefore, audible sound can be used as a simple tool to promote Protein Crystallization. In addition, the processing of other types of materials may also be affected by audible sound.
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An ignored variable: solution preparation temperature in Protein Crystallization
Scientific reports, 2015Co-Authors: Rui-qing Chen, Chen-yan Zhang, Yong-ming Liu, Hai Hou, Qing-di Cheng, Da-chuan YinAbstract:Protein Crystallization is affected by many parameters, among which certain parameters have not been well controlled. The temperature at which the Protein and precipitant solutions are mixed (i.e., the ambient temperature during mixing) is such a parameter that is typically not well controlled and is often ignored. In this paper, we show that this temperature can influence Protein Crystallization. The experimental results showed that both higher and lower mixing temperatures can enhance the success of Crystallization, which follows a parabolic curve with an increasing ambient temperature. This work illustrates that the Crystallization solution preparation temperature is also an important parameter for Protein Crystallization. Uncontrolled or poorly controlled room temperature may yield poor reproducibility in Protein Crystallization.
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Surface treatment by oxidizing the plates can alter the response of Protein Crystallization
Journal of Applied Crystallography, 2014Co-Authors: Yun-zhu Guo, Chen-yan Zhang, Yong-ming Liu, Hai Hou, Da-chuan Yin, Hui-ling Cao, Wei-hong Guo, Jian-yu ShiAbstract: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 there is no change to the routine screening protocol, this method is simple and easy to apply in Protein Crystallization.
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The effect of diluting Crystallization droplets on Protein Crystallization in vapor diffusion method
Crystal Research and Technology, 2011Co-Authors: Da-chuan Yin, Yong-ming Liu, Si-xiao Xie, Rui-qing ChenAbstract:In this study, effects of diluting either Protein or Crystallization agents in the droplets on the success rate of Protein Crystallization was investigated. Diluting the Crystallization agent was found to increase the success rate of Protein Crystallization. Theoretical analysis showed that, concentration ranges of both Protein and Crystallization agent that can be scanned during the vapor diffusion process are wider with diluting the Crystallization agent than that without dilution, resulting in more opportunities for the Crystallization solution to be in the nucleation zone. On the other hand, diluting Protein could lead to controversial results depending on the location of the initial concentration relative to that of the nucleation zone in the phase diagram. The method of diluting the Crystallization agent is therefore proposed as an alternative modification to the conventional vapor diffusion method for obtaining more Crystallization conditions in Protein Crystallization screening. (© 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim)
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Replacing a reservoir solution with desiccant in vapor diffusion Protein Crystallization screening
Journal of Applied Crystallography, 2010Co-Authors: Da-chuan Yin, Yong-ming Liu, Rui-qing Chen, Si-xiao Xie, Xian-fang Zhang, Li Zhu, Zheng-tang Liu, Peng ShangAbstract:This paper presents a modification to the conventional vapor diffusion (hanging- or sitting-drop) technique for Protein Crystallization screening. In this modified method, the reservoir solution is replaced with a desiccant to allow for a larger range of Protein solution concentrations, thereby providing more opportunities for crystal formation. This method was tested in both reproducibility and screening studies, and the results showed that it significantly improves the efficiency and reduces the cost of Protein Crystallization screens.
Yanwei Jia - One of the best experts on this subject based on the ideXlab platform.
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From Surface Self-Assembly to Crystallization: Prediction of Protein Crystallization Conditions
The journal of physical chemistry. B, 2006Co-Authors: Yanwei Jia, Xiang-yang LiuAbstract:A new criterion based on surface and volume diffusion kinetics was established to predict Protein Crystallization. Similar to the layer-by-layer crystal growth process of Protein, the kinetics of the two-dimensional self-assembly of Protein at the aqueous solution surface provides a convenient and reliable way to estimate the surface integration and the volume transport during Protein Crystallization. Both the surface and diffusion kinetics were estimated based on the Protein self-assembly at the air/solution interface, which can be obtained by measuring the surface tension. A Crystallization coefficient is found to provide an effective and reliable criterion to predict Protein Crystallization conditions. This criterion has been applied to lysozyme, concanavalin A and BSA Crystallization, and it turns out to be very successful and more reliable than the second virial coefficient criterion.
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Prediction of Protein Crystallization based on interfacial and diffusion kinetics
Applied Physics Letters, 2005Co-Authors: Yanwei Jia, Xiang-yang LiuAbstract:The interfacial kinetics of Protein Crystallization was studied via the kinetics of Protein two-dimensional self-assembly. The competition between the Protein volume transport and surface integration determines whether single crystals or amorphous aggregation will occur. A kinetic coefficient was found to provide an effective and reliable criterion to predict Protein Crystallization conditions. This criterion has been applied to lysozyme, concanavalin A and BSA Crystallization, and it turned out to be very successful and more reliable than the second virial coefficient criterion.
