Small angle neutron scattering study of lysozyme solutions

Lefaucheux, F.; Robert, M.C.; Rośenman, I.

doi:10.1016/0022-0248(93)90161-o

Cited by 62 publications

(27 citation statements)

References 17 publications

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“…This is not surprising as the chance of lysozyme monomers encountering each other via a diffusive process increases rapidly with the concentration. Thus, the present data are consistent with previous reports where it has been suggested that the critical nucleus most likely consists of four monomers and that the growth unit is likely to be the octamer (Bessho et al, 1994;Kierzek et al, 1997;Boué et al, 1993;Nadarajah et al, 1995Nadarajah et al, , 1997.…”

Section: Figuresupporting

confidence: 93%

Time Dependence of Aggregation in Crystallizing Lysozyme Solutions Probed Using NMR Self-Diffusion Measurements

Price

Tsuchiya

Arata³

2001

Biophysical Journal

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The time dependence of aggregation in supersaturated lysozyme solutions was studied using pulsed-gradient spin-echo NMR diffusion measurements as a function of lysozyme concentration at pH 6.0 and 298 K in the presence of 0.5 M NaCl. The measurements provide estimates of the weight-averaged diffusion coefficient of the monomeric to intermediate molecular weight lysozyme species present in the solution (very large aggregates and crystals are excluded from the average due to the NMR relaxation-weighting effects inherent in the method). The results show that the average molecular weight of the various lysozyme aggregates changed with sigmoidal kinetics and that these kinetics were strongly influenced by the initial lysozyme concentration. The visualization of the time dependence of the protein aggregation afforded by this method provides a deeper understanding of how the crystallizing conditions (especially the initial protein concentration) are related to the resulting crystals.

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Section: Figuresupporting

confidence: 93%

Time Dependence of Aggregation in Crystallizing Lysozyme Solutions Probed Using NMR Self-Diffusion Measurements

Price

Tsuchiya

Arata³

2001

Biophysical Journal

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“…The FITC, isomer I, octamer, while that for insulin is a hexamer, and there is evidence that lysozyme octamers and insulin hexamers are ú90% purity, was also purchased from Sigma. The labeling reaction was carried out in 0.1 M sodium carbonate solution present under crystallization conditions (11, 13,14). Aggregation can be considered as the assembly of a solute to form at pH 9.1 for 30 min at room temperature.…”

Section: Methodsmentioning

confidence: 99%

Interfacial Aggregation of Bovine Serum Albumin Related to Crystallization Conditions Studied by Total Internal Reflection Fluorescence

Asanov

DeLucas

Oldham

et al. 1997

Journal of Colloid and Interface Science

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“…The aggregates are formed even in undersaturated solutions and the extent of aggregation increases with supersaturation. Under crystal growth conditions in supersaturated solutions, the higher order aggregates predominate (Bou6, Lefaucheux, Robert & Rosenman, 1993;Behlke & Knespel, 1996). The necessary crystallizing units, therefore, already exist in bulk solution under growth conditions.…”

Section: Formation Of the Cr3'stallizing Unitsmentioning

confidence: 99%

Growth Mechanism and Morphology of Tetragonal Lysozyme Crystals

Nadarajah¹,

Pusey²

1996

Acta Cryst D

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The tetragonal form of hen egg-white lysozyme is the most investigated protein crystal for growth studies, but the relationship between its surface morphology and internal structure is still not well understood. One method of determining this relationship for inorganic crystals is by employing the periodic bond chain (PBC) theory of Hartman & Perdok [Hartman & Perdok (1955).Acta Co'st. 8,[49][50][51][52][521][522][523][524][525][526][527][528][529]. However, complexities resulting from the packing arrangements and the number of intermolecular bonds in protein crystals have resulted in the use of only simplified versions of this theory so far. In this study a more complete PBC analysis of tetragonal lysozyme crystals was carried out, coupled with an approach incorporating the molecular orientations of the crystal structure. The analysis revealed the existence of a helical tetramer building block of the entire crystal structure, centered around the 43 crystallographic axes, resulting in doublelayered slices and PBC's throughout. The analysis also indicated that the crystallizing units for the faces are at least as large as this tetramer, with the experimental evidence suggesting that it is a tetramer unit for the { 101 } faces and an octamer unit for the {110} faces. The { 110} faces were shown to be molecularly smooth F faces, while the { 101 } to be essentially rough S faces. The predicted morphology and growth mechanisms were found to explain numerous experimental observations from electron and atomic force microscopy, etching studies, lysozyme aggregation studies and measurements of growth kinetics.

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Small angle neutron scattering study of lysozyme solutions

Cited by 62 publications

References 17 publications

Time Dependence of Aggregation in Crystallizing Lysozyme Solutions Probed Using NMR Self-Diffusion Measurements

Time Dependence of Aggregation in Crystallizing Lysozyme Solutions Probed Using NMR Self-Diffusion Measurements

Interfacial Aggregation of Bovine Serum Albumin Related to Crystallization Conditions Studied by Total Internal Reflection Fluorescence

Growth Mechanism and Morphology of Tetragonal Lysozyme Crystals

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