Determination of monomer concentrations in crystallizing lysozyme solutions

Wilson, Lori J.; Pusey, Marc L.

doi:10.1016/0022-0248(92)90220-d

Cited by 30 publications

(17 citation statements)

References 18 publications

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“…The presence of lysozyme aggregates in solution have been shown by several investigators employing a variety of experimental methods (Sophianopoulos & Van Holde, 1964;Sophianopoulos, 1969;Zehavi & Lustig, 1971;Studebaker, Sykes & Wien, 1971;Banerjee, Pogolotti & Rupley, 1975;Hampe, Tondo & Hasson-Voloch, 1982;Pusey, 1991;Wilson & Pusey, 1992). The aggregates are formed even in undersaturated solutions and the extent of aggregation increases with supersaturation.…”

Section: Formation Of the Cr3'stallizing Unitsmentioning

confidence: 97%

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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Section: Formation Of the Cr3'stallizing Unitsmentioning

confidence: 97%

Growth Mechanism and Morphology of Tetragonal Lysozyme Crystals

Nadarajah¹,

Pusey²

1996

Acta Cryst D

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“…[1,3,6,7,12] and this work), the unit cell sized growth steps found on the lysozyme crystal faces [1], and the large degree of aggregation which has been observed, even below the saturation concentration, by light scattering intensity and dialysis kinetics measurements [16,17]. Re- …”

Section: Discussionmentioning

confidence: 99%

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

Forsythe¹,

Pusey²

1994

Journal of Crystal Growth

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“…The kinetics of protein crystal nucleation and the morphology of aggregates leading to crystallization vs. precipitation, therefore, were among the earliest targets of fundamental studies in protein crystallization [26]. A variety of experimental techniques have been used to explore protein crystal nucleation, including neutron [40] and X-ray scattering [17], video microscopy [20], nuclear magnetic resonance [14], calorimetry [9], static light scattering [28,29,52] and, most prominently, dynamic light scattering [21,[24][25][26]32,36,53]. The results of these and other studies, however, have often remained contradictory and controversial.…”

Section: Introductionmentioning

confidence: 99%