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Article

Hybrid Kinetic Modelling of Protein Crystallization: Hanging Drop and Langmuir–Blodgett Conditions

by
Eugenia Pechkova
1,
Fabio Massimo Speranza
2,
Paola Ghisellini
3,
Cristina Rando
3,
Katia Barbaro
4 and
Roberto Eggenhöffner
3,*
1
Laboratories of Biophysics and Nanotechnology, Department of Experimental Medicine (DIMES), University of Genova Medical School, Via A. Pastore, 3, 16132 Genova, Italy
2
Independent Researcher, 16147 Genova, Italy
3
Department of Surgical Sciences and Integrated Diagnostics (DISC), Genova University, Corso Europa 30, 16132 Genova, Italy
4
Istituto Zooprofilattico Sperimentale del Lazio e della Toscana “M. Aleandri”, Via Appia Nuova 1411, 00178 Rome, Italy
*
Author to whom correspondence should be addressed.
Crystals 2025, 15(10), 857; https://doi.org/10.3390/cryst15100857
Submission received: 2 September 2025 / Revised: 25 September 2025 / Accepted: 26 September 2025 / Published: 30 September 2025
(This article belongs to the Section Biomolecular Crystals)

Abstract

The understanding and control of protein crystallization are crucial in structural biology, drug development, and biomaterial design. This study introduces a unified framework for modeling and comparing crystallization kinetics using selected growth functions. Experimental datasets from the literature for four proteins, Lysozyme, Thaumatin, Ribonuclease A, and Proteinase K, under Hanging Drop and Langmuir–Blodgett conditions were analyzed. Five kinetic models, Avrami, Kashchiev, Hill, Logistic, and Generalized Sigmoid (GSM), were fitted to size–time data of the four benchmark proteins. From each fit, four descriptors were extracted: crystallization half-time, time of maximum growth, width at half-maximum, and peak growth rate. These metrics summarize crystallization dynamics and enable cross-comparison of proteins and methods. Langmuir–Blodgett templating accelerated onset and improved synchrony, though the effect varied by protein and model. Logistic, Hill, and GSM models provided consistent fits across most conditions, while Avrami and Kashchiev were more sensitive to early or late deviations. Notably, descriptor extraction remained reliable even with limited or uneven sampling, revealing kinetic regimes such as synchrony, asymmetry, or prolonged nucleation, not evident in raw data. This transferable analytical framework supports quantitative evaluation of crystallization behavior, aiding screening, process optimization, and time-resolved structural studies.
Keywords: crystallization kinetics; Hanging Drop method; Langmuir–Blodgett templating; kinetic modeling; nucleation descriptors crystallization kinetics; Hanging Drop method; Langmuir–Blodgett templating; kinetic modeling; nucleation descriptors

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MDPI and ACS Style

Pechkova, E.; Speranza, F.M.; Ghisellini, P.; Rando, C.; Barbaro, K.; Eggenhöffner, R. Hybrid Kinetic Modelling of Protein Crystallization: Hanging Drop and Langmuir–Blodgett Conditions. Crystals 2025, 15, 857. https://doi.org/10.3390/cryst15100857

AMA Style

Pechkova E, Speranza FM, Ghisellini P, Rando C, Barbaro K, Eggenhöffner R. Hybrid Kinetic Modelling of Protein Crystallization: Hanging Drop and Langmuir–Blodgett Conditions. Crystals. 2025; 15(10):857. https://doi.org/10.3390/cryst15100857

Chicago/Turabian Style

Pechkova, Eugenia, Fabio Massimo Speranza, Paola Ghisellini, Cristina Rando, Katia Barbaro, and Roberto Eggenhöffner. 2025. "Hybrid Kinetic Modelling of Protein Crystallization: Hanging Drop and Langmuir–Blodgett Conditions" Crystals 15, no. 10: 857. https://doi.org/10.3390/cryst15100857

APA Style

Pechkova, E., Speranza, F. M., Ghisellini, P., Rando, C., Barbaro, K., & Eggenhöffner, R. (2025). Hybrid Kinetic Modelling of Protein Crystallization: Hanging Drop and Langmuir–Blodgett Conditions. Crystals, 15(10), 857. https://doi.org/10.3390/cryst15100857

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