Diffusion coefficient of the protein in various crystallization solutions: The key to growing high-quality crystals in space

Tanaka, Hiroaki; Takahashi, Sachiko; Yamanaka, Masao; Yoshizaki, Izumi; Satô, Masaru; Сано, С.; Motohara, M.; Kobayashi, Tomoyuki; Yoshitomi, Susumu; Tanaka, Tetsuo; Fukuyama, Seijiro

doi:10.1007/bf02870387

Cited by 22 publications

(24 citation statements)

References 4 publications

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“…24,29 For proteins under macromolecular crowding the applicability of the GSE relationship is either confirmed 10,30,31 or shown to be invalid, 31,32 depending on the specific proteins and crowding agents used. 39,40 Thus, in the presence of random-coil polymers, protein diffusion is often 33,36,37,41,42 but not always 34 found to be faster than predicted by the solution viscosity, because the latter is much more affected by entanglement effects than the local diffusivity. size polydispersity.…”

Section: Introductionmentioning

confidence: 99%

Transient binding accounts for apparent violation of the generalized Stokes–Einstein relation in crowded protein solutions

Rothe

Gruber

Gröger

et al. 2016

Phys. Chem. Chem. Phys.

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The effect of high concentration, also referred to as crowding conditions, on Brownian motion is of central relevance for the understanding of the physical, chemical and biological properties of proteins in their native environment. Specifically, the simple inverse relationship between the translational diffusion coefficient and the macroscopic solution viscosity as predicted by the generalized Stokes-Einstein (GSE) relation has been the subject of many studies, yet a consensus on its applicability has not been reached. Here, we use isotope-filtered pulsed-field gradient NMR to separately assess the μm-scale diffusivity of two proteins, BSA and an SH3 domain, in mixtures as well as single-protein solutions, and demonstrate that transient binding can account for an apparent violation of the GSE relation. Whereas GSE behavior applies for the single-protein solutions, it does not hold for the protein mixtures. Transient binding behavior in the concentrated mixtures is evidenced by calorimetric experiments and by a significantly increased apparent activation energy of diffusion. In contrast, the temperature dependence of the viscosity, as well as of the diffusivity in single-component solutions, is always dominated by the flow activation energy of pure water. As a practically relevant second result, we further show that, for high protein concentrations, the diffusion of small molecules such as dioxane or water is not generally a suitable probe for the viscosity experienced by the diffusing proteins.

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Section: Introductionmentioning

confidence: 99%

Transient binding accounts for apparent violation of the generalized Stokes–Einstein relation in crowded protein solutions

Rothe

Gruber

Gröger

et al. 2016

Phys. Chem. Chem. Phys.

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show abstract

“…In this study, we used PEG 8000, because of its high viscosity, to reduce D. A 20% PEG 8000 solution behaves like a non-Newtonian fluid and the actual effect of the viscosity change caused by PEG does not decrease D by very much. Nonetheless, the viscosity coefficient of a solution containing 20% PEG 8000 is about 20 times higher than that of a pure aqueous solution (Tanaka et al, 2006). In this study, PEG 8000 was a suitable viscous reagent because it had no influence on the crystallization.…”

Section: Resultsmentioning

confidence: 78%

Crystallization of the archaeal transcription termination factor NusA: a significant decrease in twinning under microgravity conditions

et al. 2007

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The transcription termination factor NusA from Aeropyrum pernix was crystallized using a counter-diffusion technique in both terrestrial and microgravity environments. Crystallization under microgravity conditions significantly reduced the twinning content (1.0%) compared with terrestrially grown crystals (18.3%) and improved the maximum resolution from 3.0 to 2.29 Å , with similar unit-cell parameters. Based on a comparison of the crystal parameters, the effect of microgravity on protein crystallization is discussed.

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“…By the way, diffusion of protein molecules is greatly reduced in PEG, whereas diffusion of low molecular weight compounds does not slow-down in PEG [32]. Therefore, when a PEG type crystallization reagent is applied to the CD method, diffusion leakage of protein from the capillary can be suppressed, which is preferable.…”

Section: Counter-diffusion Methodsmentioning

confidence: 99%

“…The authors devised an approximate expression [32] which roughly estimates D, and an experimental method which roughly estimates β, [51,52]. In evaluating the results of the space experiment in JAXA using this index, when D/β was 3 mm or less, there was an effect of microgravity in about 70% of the crystals such as improvement of clustering and improvement of X-ray diffraction resolution [53].…”

Section: Space Experiments Modelmentioning

confidence: 99%

Methods to Grow better Diffractive Protein Crystals Acquired through Space Experiments

Hashizume¹,

Inaka²,

Furubayashi³

et al. 2019

Preprint

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Diffusion coefficient of the protein in various crystallization solutions: The key to growing high-quality crystals in space

Cited by 22 publications

References 4 publications

Transient binding accounts for apparent violation of the generalized Stokes–Einstein relation in crowded protein solutions

Transient binding accounts for apparent violation of the generalized Stokes–Einstein relation in crowded protein solutions

Crystallization of the archaeal transcription termination factor NusA: a significant decrease in twinning under microgravity conditions

Methods to Grow better Diffractive Protein Crystals Acquired through Space Experiments

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