The effects of temperature and NaCl concentration on tetragonal lysozyme face growth rates

Forsythe, Elizabeth L.; Pusey, Marc L.

doi:10.1016/0022-0248(94)90032-9

Cited by 66 publications

(56 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies using Michelson interferometry suggested a significant impurity effect on the (101) face growth rate with the presence of a pronounced dead zone [7]. However, averaged face growth rate measurements, using chromatographically repurified protein, were found to be virtually identical to those obtained previously using material prepared by dialysis and recrystallization only [11,12].…”

mentioning

confidence: 67%

See 1 more Smart Citation

Effects of purification on the crystallization of lysozyme

Ewing

Forsythe

Woerd

et al. 1996

Journal of Crystal Growth

View full text Add to dashboard Cite

mentioning

confidence: 67%

“…The plates were sealed with clear tape and incubated at 20 + 0.5°C. Crystal face growth rate measurements were performed using the techniques and instrumentation previously described [25,26].…”

Section: Protein Moleculesmentioning

confidence: 99%

Effects of purification on the crystallization of lysozyme

Ewing

Forsythe

Woerd

et al. 1996

Journal of Crystal Growth

View full text Add to dashboard Cite

“…At these conditions, the growth rates of pyramidal {101} faces were alike [15], in spite of the large scatter of the data [16] reported for pH 4.0. However, lysozyme crystallization behavior may often differ even among different batches of the same commercial protein.…”

Section: Crystal Growthmentioning

confidence: 82%

Probabilistic approach to lysozyme crystal nucleation kinetics

2015

View full text Add to dashboard Cite

Nucleation of lysozyme crystals in quiescent solutions at a regime of progressive nucleation is investigated under an optical microscope at conditions of constant supersaturation. A method based on the stochastic nature of crystal nucleation and using discrete time sampling of small solution volumes for the presence or absence of detectable crystals is developed. It allows probabilities for crystal detection to be experimentally estimated. One hundred single samplings were used for each probability determination for 18 time intervals and six lysozyme concentrations. Fitting of a particular probability function to experimentally obtained data made possible the direct evaluation of stationary rates for lysozyme crystal nucleation, the time for growth of supernuclei to a detectable size and probability distribution of nucleation times. Obtained stationary nucleation rates were then used for the calculation of other nucleation parameters, such as the kinetic nucleation factor, nucleus size, work for nucleus formation and effective specific surface energy of the nucleus. The experimental method itself is simple and adaptable and can be used for crystal nucleation studies of arbitrary soluble substances with known solubility at particular solution conditions.

show abstract

“…at lower supersaturations, when compared with the smoother (110) face (Durbin & Feher, 1986;Monaco & Rosenberger, 1993;Forsythe & Pusey, 1994). Perhaps more significantly, the smoothness of the (110) face is indicated by its slower dissolution rates during etching of the crystal (Monaco & Rosenberger, 1993).…”

Section: Molecular Packing On Edges and Verticesmentioning

confidence: 99%

“…Although such extensive investigations have not yet been carried out for the (101) face, the experimental evidence shows that the growth rates on this face also have a similar dependence on the supersaturation (Monaco & Rosenberger, 1993;Forsythe & Pusey, 1994). Furthermore, the (101) growth rates are higher than the (110) growth rates at lower supersaturation.…”

Section: Formation Of the Cr3'stallizing Unitsmentioning

confidence: 99%

Growth Mechanism and Morphology of Tetragonal Lysozyme Crystals

Nadarajah¹,

Pusey²

1996

Acta Cryst D

View full text Add to dashboard Cite

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.

show abstract

The effects of temperature and NaCl concentration on tetragonal lysozyme face growth rates

Cited by 66 publications

References 18 publications

Effects of purification on the crystallization of lysozyme

Effects of purification on the crystallization of lysozyme

Probabilistic approach to lysozyme crystal nucleation kinetics

Growth Mechanism and Morphology of Tetragonal Lysozyme Crystals

Contact Info

Product

Resources

About