Impurity effect on defect formation of protein crystals

Hondoh, Hironori; Nakada, T.

doi:10.1016/j.jcrysgro.2004.11.236

Cited by 9 publications

(18 citation statements)

References 19 publications

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“…In the etching process, the first appeared etch pits were deep flat-bottomed ones, the number of which kept constant in the whole etching process. This result was the same as that of Hondoh et al [9,10], showing that the observation of etch pits caused by micro-impurities using phase contrast microscopy was feasible. Moreover, we found that the number of flat-bottomed etch pits gradually increased with the etching time within 40 min.…”

Section: Observation Of Etch Pits By the Optical Methodssupporting

confidence: 88%

“…Micro-impurity molecules affect protein crystal quality although their concentration in protein solution is low. For example, the point defects caused by the adsorption of microimpurities on crystal surface strongly affect the crystal quality [9,10]. However, until now only a very small number of works focus on micro-impurity in protein crystallization.…”

Section: Introductionmentioning

confidence: 99%

“…The etch figure method, which is usually applied in inorganic material studies, has been applied in protein crystallization research recently. In 2004, Hondoh et al [9,10] studied the surface morphology of lysozyme crystals after etching by AFM. They found three types of etch pits: flat-bottomed type, deep flatbottomed type, and point-bottomed type.…”

Section: Introductionmentioning

confidence: 99%

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Influence of micro-impurity on protein crystal growth studied by the etch figure method

Dai

Liu

Sazaki

et al. 2009

Journal of Crystal Growth

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a b s t r a c tThe investigation of the effect of micro impurity on crystal growth by optical microscopy has been validated. The results showed that the growth rate of a lysozyme crystal was affected even if the concentration of impurity of fluorescent-labeled lysozyme (abbreviation, F-lysozyme) was very small. Different concentrations of F-lysozyme had different effects on crystal growth rate. The growth rate decreased much more as F-lysozyme concentration increased. The density of incorporated F-lysozyme on different grown layers of a lysozyme crystal during crystal growth was obtained from the results of flat-bottomed etch pits density.

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Section: Observation Of Etch Pits By the Optical Methodssupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Influence of micro-impurity on protein crystal growth studied by the etch figure method

Dai

Liu

Sazaki

et al. 2009

Journal of Crystal Growth

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“…[17][18][19][20][21][22][23][24] Generally, impurities are considered to exhibit their effects on the growth process after they adsorb on a crystal surface. Thus, to fully comprehend the mechanisms of impurity effects, one has to observe in situ both (1) dynamics of elementary steps and (2) adsorption of impure molecules on a crystal surface, at a molecular level.…”

Section: Introductionmentioning

confidence: 99%

Direct Observation of Adsorption Sites of Protein Impurities and Their Effects on Step Advancement of Protein Crystals

Sazaki

戴国亮

et al. 2009

Crystal Growth & Design

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ABSTRACT:We measured noninvasively step velocities of elementary two-dimensional (2D) islands on {110} faces of tetragonal lysozyme crystals, under various supersaturations, by laser confocal microscopy combined with differential interference contrast microscopy. We studied the correlation between the effects of protein impurities on the growth of elementary steps and their adsorption sites on a crystal surface, using three kinds of proteins: fluorescent-labeled lysozyme (F-lysozyme), covalently bonded dimers of lysozyme (dimer), and a 18 kDa polypeptide (18 kDa). These three protein impurities suppressed the advancement of the steps. However, they exhibited different supersaturation dependencies of the suppression of the step velocities. To clarify the cause of this difference, we observed in situ the adsorption sites of individual molecules of F-lysozyme and fluorescent-labeled dimer (F-dimer) on the crystal surface by single-molecule visualization. We found that F-lysozyme adsorbed preferentially on steps (i.e., kinks), whereas F-dimer adsorbed randomly on terraces. Taking into account the different adsorption sites of F-lysozyme and F-dimer, we could successfully explain the different effects of the impurities on the step velocities. These observations strongly suggest that 18 kDa also adsorbs randomly on terraces. Seikagaku lysozyme exhibited a complex effect that could not alone be explained by the two major impurities (dimer and 18 kDa) present in Seikagaku lysozyme, indicating that trace amounts of other impurities significantly affect the step advancement.

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“…The effect of impurities on protein crystal growth has been intensively studied, and its influence on crystal perfection has recently been investigated [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19]. The crystal perfection was evaluated by various methods such as X-ray diffraction (maximum resolution or overall B-factor: i.e., a factor used to evaluate the crystal quality in the field of protein crystal growth and is obtained from the Wilson Plot [20,21]) [8,9,11,15,18], atomic force microscope (AFM) [7,14,18], fluorescence methods [11][12][13]17], rocking curve measurement [11], X-ray topography [5,11], and etching [19].…”

Section: Introductionmentioning

confidence: 99%