Observation of growth steps, spiral dislocations and molecular packing on the surface of lysozyme crystals with the atomic force microscope

Konnert, J. H.; D’Antonio, Peter; Ward, Keith B.

doi:10.1107/s0907444994001988

Cited by 73 publications

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“…The step height presumably corresponds to the unimolecular growth layers observed on this face (Durbin & Feher, 1990;Durbin & Carlson, 1992). Unfortunately, Durbin and coworkers do not report growth step heights as were reported for the (110) face by Konnert et al (1994). Nevertheless, 34.2 A Ê is much closer than 17.1 A Ê to the 28.0 Â 28.0 Â 37.9 A Ê dimensions of single lysozyme molecules as shown in Fig.…”

Section: Growth Mechanism and Surface Morphologymentioning

confidence: 72%

“…It was also shown that the 4 3 helix is formed by strong bonds and that crystal growth is likely to proceed in a manner which preserves this unit's structure. These predictions were con®rmed by AFM scans which showed that the (110) faces are formed by planes corresponding to this construction (Konnert et al, 1994;Li, Perozzo et al, 1999). Further con®rmation was provided by a recent study of the crystal-packing arrangement employing a somewhat different approach (Strom & Bennema, 1997a,b).…”

Section: Growth Mechanism and Surface Morphologymentioning

confidence: 82%

“…Growth units of at least tetramer size are needed to preserve the completeness of the 4 3 helices in the crystal, which is a requirement for both the (110) and (101) faces (Nadarajah & Pusey, 1996;Strom & Bennema, 1997a,b). As mentioned previously, only complete 4 3 helices were found on the (110) face in AFM investigations (Konnert et al, 1994;Li, Perozzo et al, 1999). This requirement also rules out larger crystallizing units for this face, as this would have resulted in the growth steps being multi-layered.…”

Section: Growth Mechanism and Surface Morphologymentioning

confidence: 98%

“…Some units were as large as dodecamers. Earlier AFM and electron-microscopy studies have shown that growth by multilayers is a common occurrence on both (101) and (110) faces (Durbin & Feher, 1990;Durbin & Carlson, 1992;Konnert et al, 1994). Additionally, several studies have shown that the (101) face grows faster than the (110) face at lower supersaturations and grows more slowly than the (110) face at higher supersaturations (Durbin & Feher, 1986;Forsythe et al, 1999).…”

Section: Growth Mechanism and Surface Morphologymentioning

confidence: 99%

“…This relationship then allowed the molecular-growth mechanism of the crystal face to be deduced and the results to be con®rmed from atomic force microscopy (AFM) and electron-microscopy studies. These analyses revealed that tetragonal lysozyme crystals were constructed by helices centered around the 4 3 axes, consisting of four molecules in a single turn (Konnert et al, 1994;Li, Perozzo et al, 1999). The growth mechanism was shown to proceed by the addition to the (110) face of a variety of growth units corresponding to these helices .…”

Section: Introductionmentioning

confidence: 99%

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Growth of (101) faces of tetragonal lysozyme crystals: determination of the growth mechanism

Nadarajah

Pusey

1999

Acta Crystallogr D Biol Cryst

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Measurements of the macroscopic growth rates of the (101) face of tetragonal lysozyme crystals indicate an unusual dependence on the supersaturation [Forsythe et al. (1999), Acta Cryst. D55, 1005±1011] similar to that observed for the (110) face. As performed previously for the (110) face, the surface packing arrangement for the (101) face was constructed in this study based on earlier microscopic observations and theoretical analysis of the internal molecular packing. This allowed the minimum growth unit for this face to be identi®ed as a tetramer corresponding to a single turn of helices centered about the 4 3 axes and the minimum growth step to be identi®ed as of unimolecular height. A macroscopic mathematical model for the growth of the (101) face was developed based on the reversible formation of multimeric growth units in solution and the addition of a unit to the crystal face by dislocation and two-dimensional nucleation mechanisms. The calculations showed that the best ®ts were obtained for tetramer or octamer growth units in this model. This and other evidence suggests that while growth may proceed by a variety of growth units, the average size of these units is between that of a tetramer and an octamer.

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Section: Growth Mechanism and Surface Morphologymentioning

confidence: 72%

Section: Growth Mechanism and Surface Morphologymentioning

confidence: 82%

Section: Growth Mechanism and Surface Morphologymentioning

confidence: 98%

Section: Growth Mechanism and Surface Morphologymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Growth of (101) faces of tetragonal lysozyme crystals: determination of the growth mechanism

Nadarajah

Pusey

1999

Acta Crystallogr D Biol Cryst

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Proteins as a Key to Advanced Crystal Growth Studies

Rosenberger¹

1999

Cryst. Res. Technol.

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Extended AbstractOver the last decade, extensive advances have been made in the understanding of protein crystallization; for summaries see ROSENBERGER, ROSENBERGER et al.. Proteins crystallize by layer spreading mechanisms. This is macroscopically indicated by well developed facets that are often observed. On a molecular level, layer growth has been revealed by electron microscopy (DURBIN, FEHER) and atomic force microscopy studies (DURBIN et al.; KONNERT et al.; MCPHERSON et al.; LAND et al.; MALKIN et al.) that reproduced the whole body of morphology scenarios known for crystallization from inorganic solutions. These include layer spreading from dislocations and 2D nuclei, interaction of growth steps from sources of different activity, and impediment of step propagation by impurities and foreign particles.Since the earliest kinetics investigations it has become apparent that protein crystal growth is more controlled by interfacial kinetics than by bulk transport; for references see ROSENBERGER et al.. Furthermore, two to three orders of magnitude higher supersaturations are required than in inorganic solution growth, to obtain comparable growth rates. Due to these slow kinetics and the large size of the solute macro-ions (crystal building blocks) involved, the interplay between the bulk transport-dependent supply of solute and impurities and the interfacial kinetics can be investigated by conventional optical means. Thus, proteins present ideal model systems for advanced crystal growth studies Particularly detailed insight on the growth kinetics has been obtained from in-situ highresolution interferometric microscopy (VEKILOV et al., 1995a), which permits the simultaneous acquisition of practically continuous time traces of the normal growth rate R and vicinal slope p at various locations across whole crystal faces. Since p is proportional to the local growth step density, these observations permit correlations between the bulk transport, that can be modified, and the microscopic morphological response in the form of the spatio-temporal changes in step motion.The results, when time-averaged over periods of the order of ten minutes reveal the pertinence of all intrinsic and impurity-induced kinetics mechanisms observed in inorganic systems VEKILOV et al., 1995b;LIN et al.;. However, utilization of the high temporal resolution afforded by this advanced interferometric technique, resulted in a new understanding of step propagation. It was found that even under highly stable external solution conditions, both R and p undergo strong fluctuations with a characteristic time of a few minutes . The unsteadiness in p reveals that the fluctuations are due to the bunching and debunching of

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In situ measurement of crystal surface dynamics in pure and contaminated solutions by Confocal Microscopy and Atomic Force Microscopy

Driessche

Sleutel

2013

Crystal Research and Technology

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Impurities are omnipresent during crystallization from solution, both in the lab and in natural environments. Unravelling the mechanisms of impurity effects during crystal growth contributes to the general understanding of crystallization processes and our ability to control it. One way of obtaining information on the impurity mechanisms is to observe the interaction of these foreign species with the growth sites in situ, if possible at a molecular level. At present several optical based techniques are being employed for this type of research. In this chapter, the application of two popular methods in the area of crystal growth observation, atomic force microscopy and confocal microscopy, will be discussed, pointing out the strong points of each technique illustrated with examples from literature and the authors own work. The aim of this chapter is to show experimentalists, venturing into the field of crystal growth, the wide array of research possibilities these techniques offer for exploring the intriguing world of impurity interactions with crystalline materials.

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Observation of growth steps, spiral dislocations and molecular packing on the surface of lysozyme crystals with the atomic force microscope

Cited by 73 publications

References 0 publications

Growth of (101) faces of tetragonal lysozyme crystals: determination of the growth mechanism

Growth of (101) faces of tetragonal lysozyme crystals: determination of the growth mechanism

Proteins as a Key to Advanced Crystal Growth Studies

In situ measurement of crystal surface dynamics in pure and contaminated solutions by Confocal Microscopy and Atomic Force Microscopy

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