Heterogeneous nucleation (and adhesion) of lysozyme crystals

Tsekova, D.; Dimitrova, Sonya; Nanev, Christo N.

doi:10.1016/s0022-0248(98)00827-6

Cited by 73 publications

(110 citation statements)

References 16 publications

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“…Additional research is necessary in this respect. The results may be of interest also for the discussion of the heterogeneous crystal nucleation [7].…”

Section: Resultsmentioning

confidence: 83%

“…Some preliminary data (resulting from our investigations several years ago) for the adhesion of tetragonal hen-egg white lysozyme, HEWL crystals are already reported [7]. Meanwhile, many additional measurements are being performed and the refined data are presented now.…”

Section: Introductionmentioning

confidence: 93%

“…As already mentioned the constant C is determined individually, by weighing, for every glass fibre. The rough approximation, to ascribe the total work A def to the adhesion energy [7], yields rather big values. It is evident that, besides the surface energy of the two new surfaces which appear after crystal detachment, several additional components are included in the stress energy, calculated by means of eq.…”

Section: Adhesion Energymentioning

confidence: 99%

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Adhesion of protein crystals: Measurement of the detachment force

Nanev¹,

Dimitrov²,

Tsekova³

2006

Cryst. Res. Technol.

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The degree of adhesion of protein crystals, heterogeneously nucleated and grown on different supports (e.g. glass plates and plates coated with poly-L-lysine, hexamethyl-disilazane and silicon) is measured directly with a purposely-developed technique. The sticking force crystal/support is determined by means of a flexible glass fibre, which bending is calibrated by means of series of weights. In this way an elastic constant, specific for each glass fiber is determined individually. Appropriate glass fibres with relative bending less than 10% (Hook's law) are used. The force which is necessary to be exerted, by means of a micro-manipulator, in order to detach the crystal from the support is taken as a quantitative measure for the adhesion strength. Forces between 10 N cm -2 and 1 N cm -2 for differently oriented tetragonal hen-egg-white lysozyme and cubic ferritin crystals, and 0.1 N cm -2 for rhombohedral (porcine) insulin and orthorhombic trypsin crystals are measured. The tetragonal HEWL and rhombohedral insulin crystals show anisotropy of the adhesion strength. In contrast, the cubic ferritin crystals are isotropic also in this respect. For comparison purposes adhesion measurements are performed with NaCl and sugar crystals. An attempt is made to evaluate also the adhesion energy of the protein crystals.

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“…Additional research is necessary in this respect. The results may be of interest also for the discussion of the heterogeneous crystal nucleation [7].…”

Section: Resultsmentioning

confidence: 83%

Section: Introductionmentioning

confidence: 93%

Section: Adhesion Energymentioning

confidence: 99%

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Adhesion of protein crystals: Measurement of the detachment force

Nanev¹,

Dimitrov²,

Tsekova³

2006

Cryst. Res. Technol.

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“…It should be noted however that the proper fulfillment of the procedure requires some experimental skills, e.g. see [4,[11][12][13].…”

Section: Methodsmentioning

confidence: 99%

Heterogeneous versus bulk nucleation of lysozyme crystals

Hodzhaoglu

Nanev²

2010

Cryst. Res. Technol.

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Heterogeneous (on-glass) protein crystal nucleation was separated from the bulk one in systems of thin protein solution layers, confined between two glass plates of custom made quasi two-dimensional all-glass cells, as well as by applying forced protein solution flow. Two commercial samples of hen-egg-white lysozyme, Seikagaku and Sigma were used as model proteins. Applying the classical technique of separation in time of nucleation and growth stages with protein solution layers of thickness 0.05 cm we found that the on-glass crystal nucleation prevailed highly with Seikagaku HEWL, while on the opposite, bulk nucleated crystals represented the main crystal fraction in Sigma solution. Also using 0.05 cm solution layers nucleation rates were measured separately for the on-glass and bulk protein crystals. The process was investigated by varying solution layer thicknesses as well, from 0.05 down to 0.01, 0.0065 and 0.002 cm. Studying the influence of the forced protein solution flow on HEWL crystal nucleation the classical double-pulse technique was modified by separating the nucleation and growth stages not only in time, but simultaneously also in place. In this case we found that the ratio of on-glass formed crystal nuclei to bulk nuclei depended on the flow velocity, but in different manner with Seikagaku HEWL and Sigma HEWL. A plausible explanation of our experimental results is that the bulk crystal nucleation occurs on foreign surfaces as well, e.g. on rests of source biomaterial, which are always present in the protein solutions. Moreover, biomaterial seems to be more active nucleant than glass.

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“…-The Double Pulse Technique (DPT), which permits nucleation and growth to be separated [37][38][39]. At the beginning of a run, the solution is loaded at a temperature chosen to prevent nucleation of crystals.…”

Section: Experimental Considerationsmentioning

confidence: 99%