Characterization of dislocations in monoclinic hen egg-white lysozyme crystals by synchrotron monochromatic-beam X-ray topography

Sawaura, Takuya; Fujii, Daiki; Shen, Mengyuan; Yamamoto, Yu; Wako, Kei; Kojima, K.; Tachibana, Masaru

doi:10.1016/j.jcrysgro.2010.11.018

Cited by 17 publications

(12 citation statements)

References 14 publications

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“…Research concerning the origins of disorder, i.e. imperfection in protein crystals, has been actively performed by several groups (Snell et al, 1995;Dobrianova et al, 1998;Izumi et al, 1999;Fourme et al, 1999;Otalora et al, 1999;Caylor et al, 1999;Boggon et al, 2000;Capelle et al, 2004;Hu et al, 2004;Yoshizaki et al, 2006;Koishi et al, 2007;Mukobayashi et al, 2009;Sawaura et al, 2011). This research has revealed that the impurities and dislocations have a significant effect on the crystal quality of proteins.…”

Section: Thermodynamic Effect Of An External Electric Field On Entropymentioning

confidence: 99%

Improvement of crystal quality for tetragonal hen egg white lysozyme crystals under application of an external alternating current electric field

et al. 2013

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X-ray diffraction rocking-curve measurements were performed on tetragonal hen egg white lysozyme (HEWL) crystals grown with and without application of an external alternating current (AC) electric field, and then the crystal quality was assessed by the FWHMs of each rocking-curve profile. The FWHMs for HEWL crystals grown with an external electric field were smaller than those for crystals grown without. In particular, the average FWHM for the 12 12 0 reflection with an external electric field (0.0034 ) was significantly smaller than that without (0.0061 ). This indicates that the crystal quality of HEWL crystals was improved by application of the external AC electric field. This crystallization technique can be expected to enhance the resolution of protein molecule structure analysis by X-ray diffraction.

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Section: Thermodynamic Effect Of An External Electric Field On Entropymentioning

confidence: 99%

Improvement of crystal quality for tetragonal hen egg white lysozyme crystals under application of an external alternating current electric field

et al. 2013

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“…In particular, it is thermodynamically analyzed that the entropy of the solid decreases under an applied electric field at 1 MHz, and therefore, a decrease of disorder in the crystal could be expected. Several groups have actively attempted the elucidation of the origins of disorder, i.e., imperfection in protein crystals [11,[55][56][57][58][59][60][61][62][63][64][65][66], leading to the results that impurities and dislocations have an undesirable influence on the crystal quality of proteins. However, the origins of imperfections in protein crystals are not completely comprehended.…”

Section: Introductionmentioning

confidence: 99%

Technique for High-Quality Protein Crystal Growth by Control of Subgrain Formation under an External Electric Field

et al. 2016

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X-ray diffraction (XRD) rocking-curves were measured for tetragonal hen egg white (HEW) lysozyme crystals grown with and without application of an external electric field, and the crystal quality was assessed according to the full width at half-maximums (FWHMs) of each rocking-curve profile. The average FWHMs for tetragonal HEW lysozyme crystals grown with an external electric field at 1 MHz were smaller than those for crystals grown without, especially for the 12 12 0 reflection. The crystal homogeneity of the tetragonal HEW lysozyme crystals was also improved under application of an external electric field at 1 MHz, compared to that without. Improvement of the crystal quality of tetragonal HEW lysozyme crystals grown under an applied field is discussed with a focus on subgrain formation. In addition, the origin of subgrain misorientation is also discussed with respect to the incorporation of impurities into protein crystals.

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“…It was reported that the growth of the middle and outer sections of a crystal are influenced by the molecular order of the inner section of the crystal as shown with X-ray tomography (Sawaura et al, 2011). Therefore, we speculate that the outer section of crystals grown in TDM may have better quality because the supersaturation ratios and impurity concentrations are lower in the inner section of the crystals grown in TDM than those of the crystals grown in THM.…”

Section: Resultsmentioning

confidence: 73%

Numerical model of protein crystal growth in a diffusive field such as the microgravity environment

Tanaka

Sasaki²,

Takahashi

et al. 2013

J Synchrotron Rad

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It is said that the microgravity environment positively affects the quality of protein crystal growth. The formation of a protein depletion zone and an impurity depletion zone due to the suppression of convection flow were thought to be the major reasons. In microgravity, the incorporation of molecules into a crystal largely depends on diffusive transport, so the incorporated molecules will be allocated in an orderly manner and the impurity uptake will be suppressed, resulting in highly ordered crystals. Previously, these effects were numerically studied in a steady state using a simplified model and it was determined that the combination of the diffusion coefficient of the protein molecule (D) and the kinetic constant for the protein molecule () could be used as an index of the extent of these depletion zones. In this report, numerical analysis of these depletion zones around a growing crystal in a non-steady (i.e. transient) state is introduced, suggesting that this model may be used for the quantitative analysis of these depletion zones in the microgravity environment.

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Characterization of dislocations in monoclinic hen egg-white lysozyme crystals by synchrotron monochromatic-beam X-ray topography

Cited by 17 publications

References 14 publications

Improvement of crystal quality for tetragonal hen egg white lysozyme crystals under application of an external alternating current electric field

Improvement of crystal quality for tetragonal hen egg white lysozyme crystals under application of an external alternating current electric field

Technique for High-Quality Protein Crystal Growth by Control of Subgrain Formation under an External Electric Field

Numerical model of protein crystal growth in a diffusive field such as the microgravity environment

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