A crystallization technique for obtaining large protein crystals with increased mechanical stability using agarose gel combined with a stirring technique

Maruyama, Mihoko; Hayashi, Yasuhiko; Yoshikawa, Hiroshi; Okada, Shino; Koizumi, Hideaki; Tachibana, Masaru; Sugiyama, Shigeru; Adachi, Hiroaki; Matsumura, Hideki; Inoue, Tsuyoshi; Takano, Kazufumi; Murakami, Satoshi; Yoshimura, Masashi; Mori, Yusuke

doi:10.1016/j.jcrysgro.2015.11.008

Cited by 10 publications

(7 citation statements)

References 40 publications

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“…The growth of high-quality single crystals of proteins has been intensively pursued using magnetic fields [3][4][5][6][7][8][9], microgravity [10][11][12][13][14][15][16], solution flow [17][18][19][20], and gel as a growth host media [21][22][23][24][25][26][27][28]. A growth technique mediated by screw dislocations under low supersaturation has also been proposed [29][30][31][32].…”

Section: Introductionmentioning

confidence: 99%

Effect of an External Electric Field on the Kinetics of Dislocation-Free Growth of Tetragonal Hen Egg White Lysozyme Crystals

et al. 2017

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Dislocation-free tetragonal hen egg white (HEW) lysozyme crystals were grown from a seed crystal in a cell. The rates of tetragonal HEW lysozyme crystal growth normal to the (110) and (101) faces with and without a 1-MHz external electric field were measured. A decrease in the typical growth rates of the crystal measured under an applied field at 1 MHz was observed, although the overall driving force increased. Assuming that the birth and spread mechanism of two-dimensional nucleation occurs, an increase in the effective surface energy of the step ends was realized in the presence of the electric field, which led to an improvement in the crystal quality of the tetragonal HEW lysozyme crystals. This article also discusses the increase in the effective surface energy of the step ends with respect to the change in the entropy of the solid.

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Section: Introductionmentioning

confidence: 99%

Effect of an External Electric Field on the Kinetics of Dislocation-Free Growth of Tetragonal Hen Egg White Lysozyme Crystals

et al. 2017

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“…These can affect the crystal nucleation and growth which are both critical to a crystallization process. Moreover, a large number of research studies have proved that the addition of TMAs is an effective strategy for regulating product properties. , Compared with other control strategies, such as the optimization of process parameters and the assistance of external fields (such as magnetic field, ultrasound, and microwave), TMAs may have more prominent advantages − because the experimental operation of adding TMAs into the solution during crystallization is simple and they play a significant role in a very small amount. Furthermore, TMAs can be carefully screened or designed to achieve the effective and flexible control of crystal properties.…”

Section: Introductionmentioning

confidence: 99%

Role of Tailor-Made Additives in Crystallization from Solution: A Review

Zhu

Gao

et al. 2023

Ind. Eng. Chem. Res.

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Additives which share a similar molecular structure with the crystallizing parent molecule are called tailor-made additives (TMAs). The inclusion of well-chosen TMAs often has a significant impact on crystallization behaviors. However, how TMAs affect the solution crystallization has seldom been systematically summarized in recent years. Herein this paper reviews the role of TMAs in solution crystallization. First, the effects and action mechanisms of TMAs on crystal nucleation and growth are discussed, respectively. Next, the applications of TMAs in the regulation of crystal properties including the polymorphism, crystal habit, crystal size, and chirality are introduced. Then the recent progress of molecular simulation in predicting the role of TMAs is discussed. Finally, we analyze the existing problems in this field and give an outlook on the future development. This paper is helpful and useful to readers interested in the use of TMAs to control crystallization and design crystals with desired properties.

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“…Therefore, it can be advantageous to produce rigid protein crystals not affected by the soaking operation into different solution conditions. Several approaches have been reported so far to improve the mechanical stability of protein crystals, including growing in a high-concentration hydrogel ( Sugiyama et al, 2012 ; Maruyama et al, 2016 ), chemical cross-linking ( Yan et al, 2015 , 2016 ; Kubiak et al, 2019 ; Nguyen et al, 2019 ), and rational design of crystal-packing contacts ( Heinz and Matthews, 1994 ; Derewenda, 2004 ; Yamada et al, 2007 ; Abe and Ueno, 2015 ; Negishi et al, 2018 ; Hermann et al, 2021 ). Considering that chemical cross-linkers sometimes cause non-specific reactions with essential residues for enzymatic activities ( Ayala et al, 2002 ), rational design such as the introduction of disulfide bridges based on the structural information could be more suitable in immobilizing protein crystals while preserving their activities.…”

Section: Introductionmentioning

confidence: 99%

Creation of Cross-Linked Crystals With Intermolecular Disulfide Bonds Connecting Symmetry-Related Molecules Allows Retention of Tertiary Structure in Different Solvent Conditions

Hiromoto

Ikura

Honjo

et al. 2022

Front. Mol. Biosci.

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Protein crystals are generally fragile and sensitive to subtle changes such as pH, ionic strength, and/or temperature in their crystallization mother liquor. Here, using T4 phage lysozyme as a model protein, the three-dimensional rigidification of protein crystals was conducted by introducing disulfide cross-links between neighboring molecules in the crystal. The effect of cross-linking on the stability of the crystals was evaluated by microscopic observation and X-ray diffraction. When soaking the obtained cross-linked crystals into a precipitant-free solution, the crystals held their shape without dissolution and diffracted to approximately 1.1 Å resolution, comparable to that of the non-cross-linked crystals. Such cross-linked crystals maintained their diffraction even when immersed in other solutions with pH values from 4 to 10, indicating that the disulfide cross-linking made the packing contacts enforced and resulted in some mechanical strength in response to changes in the preservation conditions. Furthermore, the cross-linked crystals gained stability to permit soaking into solutions containing high concentrations of organic solvents. The results suggest the possibility of obtaining protein crystals for effective drug screening by introducing appropriate cross-linked disulfide bonds.

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A crystallization technique for obtaining large protein crystals with increased mechanical stability using agarose gel combined with a stirring technique

Cited by 10 publications

References 40 publications

Effect of an External Electric Field on the Kinetics of Dislocation-Free Growth of Tetragonal Hen Egg White Lysozyme Crystals

Effect of an External Electric Field on the Kinetics of Dislocation-Free Growth of Tetragonal Hen Egg White Lysozyme Crystals

Role of Tailor-Made Additives in Crystallization from Solution: A Review

Creation of Cross-Linked Crystals With Intermolecular Disulfide Bonds Connecting Symmetry-Related Molecules Allows Retention of Tertiary Structure in Different Solvent Conditions

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