Interferometry measurement of protein concentration evolution during crystallization and dissolution with improved reliability and versatility

Yin, Da‐Chuan; Inatomi, Yuko; Luo, Hui-Min; Li, H S; Lu, Hui‐Meng; Ye, Y J; Wakayama, Nobuko I.

doi:10.1088/0957-0233/19/4/045303

Cited by 12 publications

(4 citation statements)

References 49 publications

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“…It is known that an aged supersaturated solution under isothermal conditions will undergo a concentration redistribution in solution. − Nevertheless, the solution could be more homogeneous with vibration than without. Therefore, vibration could affect the nucleation and growth behavior because the supersaturation level will be different with and without vibration.…”

Section: Discussionmentioning

confidence: 99%

Improving Protein Crystal Quality via Mechanical Vibration

Zhang

Liang

et al. 2016

Crystal Growth & Design

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Growing high quality protein crystals enables higher quality high-resolution structure determination by X-ray diffraction. In this paper, we show that mechanical vibration could be an effective and useful tool for improving protein crystal quality. The crystal quality of the selected proteins was examined using X-ray diffraction. The quality comparison of the crystals grown with and without vibration verified that mechanical vibration not only enhanced the morphology of the crystals but also improved the crystal quality. Therefore, we propose that mechanical vibration could be a useful alternative tool for obtaining high quality-diffracting protein crystals.

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Section: Discussionmentioning

confidence: 99%

Improving Protein Crystal Quality via Mechanical Vibration

Zhang

Liang

et al. 2016

Crystal Growth & Design

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“…Knowledge of the phase diagram is of key importance when designing and controlling a crystallization process (Astier & Veesler, 2008;Vekilov, 2012;Zhang et al, 2014). In the case of macromolecules such as proteins, the availability of accurate phase diagram data is limited owing to the diversity of their structures and the lack of suitable experimental setups to readily perform reliable measurements of protein solubility during crystallization using a small amount of protein sample (Garcia-Ruiz et al, 1999;Olesberg et al, 2000;Curtis et al, 2001;Asherie, 2004;Dumetz et al, 2007;Yin et al, 2008;Y. Zhang et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Optimization of crystallization of biological macromolecules using dialysis combined with temperature control

Junius¹,

Vahdatahar²,

Oksanen³

et al. 2020

J Appl Cryst

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A rational way to find the appropriate conditions to grow crystal samples for bio-crystallography is to determine the crystallization phase diagram, which allows precise control of the parameters affecting the crystal growth process. First, the nucleation is induced at supersaturated conditions close to the solubility boundary between the nucleation and metastable regions. Then, crystal growth is further achieved in the metastable zone -which is the optimal location for slow and ordered crystal expansion -by modulation of specific physical parameters. Recently, a prototype of an integrated apparatus for the rational optimization of crystal growth by mapping and manipulating temperature-precipitant-concentration phase diagrams has been constructed. Here, it is demonstrated that a thorough knowledge of the phase diagram is vital in any crystallization experiment. The relevance of the selection of the starting position and the kinetic pathway undertaken in controlling most of the final properties of the synthesized crystals is shown. The rational crystallization optimization strategies developed and presented here allow tailoring of crystal size and diffraction quality, significantly reducing the time, effort and amount of expensive protein material required for structure determination. research papers J. Appl. Cryst. (2020). 53, 686-698 Niels Junius et al. Optimization of crystallization of biological macromolecules 687 research papers J. Appl. Cryst. (2020). 53, 686-698 Niels Junius et al. Optimization of crystallization of biological macromolecules 689

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“…Интерферометрические исследования растворов можно условно разделить на те, в которых объемы исследуемых растворов порядка одного миллилитра и больше, и те, где объемы порядка одного микролитра или меньше -вплоть до мономолекулярных слов. В первом случае измерения показателя преломления проводятся, главным образом, для контроля равновесных концентраций веществ [1] или для динамического контроля во время роста кристаллов [2]. Как правило, погрешность измерения показателя преломления в таких исследованиях выше, порядка 10 −4 .…”

Section: Introductionunclassified

Прецизионная Интерферометрия Как Новый Метод Исследования Конформационного Состояния Белка И Его Взаимодействия С Растворителем

Матвеева¹,

Саримов²,

Бинги³

2020

Журнал Технической Физики

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A new method for studying the conformational state of a protein and its interaction with a solvent has been developed. The method is based on measuring the refractive index of a protein solution using a precision laser interferometer with an accuracy of 1 • 10–7. The interferometer was calibrated based on the known temperature dependence of water refractive index and concentration dependence of the refractive index of a NaCl solution. Using an interferometer, changes in the refractive index during proteolysis (an increase of 9 ∙ 10-6 and 2.4 ∙ 10-6 in the refractive index of bovine serum albumin and egg lysozyme solutions during pepsin-catalyzed hydrolysis) and denaturation (increase in the refractive index by 4.5 ∙ 10-5 during the reaction of egg lysozyme with guanidine hydrochloride and dithiothreitol) have been first recorded. Based on direct interferometric measurements, the widespread assumption has been refuted that the refractive index of protein solutions is determined only by the concentration of the protein and its amino acid composition and does not depend on the state of protein fragmentation. The increased accuracy of the interferometer allows one to study the increment of the refractive index (dn/dc) at low concentrations of dissolved compounds (<< 1%), as well as processes leading to a change in the conformation of macromolecules in solution.

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Interferometry measurement of protein concentration evolution during crystallization and dissolution with improved reliability and versatility

Cited by 12 publications

References 49 publications

Improving Protein Crystal Quality via Mechanical Vibration

Improving Protein Crystal Quality via Mechanical Vibration

Optimization of crystallization of biological macromolecules using dialysis combined with temperature control

Прецизионная Интерферометрия Как Новый Метод Исследования Конформационного Состояния Белка И Его Взаимодействия С Растворителем

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