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Mike Sleutel

Researcher at Vrije Universiteit Brussel

Publications -  42
Citations -  1039

Mike Sleutel is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Nucleation & Crystal growth. The author has an hindex of 15, co-authored 37 publications receiving 823 citations. Previous affiliations of Mike Sleutel include Flanders Institute for Biotechnology.

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Role of clusters in nonclassical nucleation and growth of protein crystals

TL;DR: Experimental evidence shows that intermediate metastable states can be liquid-like clusters that are stable with respect to the parent liquid and metastable compared with the emerging crystalline phase and that clusters existing in protein solutions can significantly increase the nucleation rate and therefore play a relevant role in theucleation process.
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Molecular nucleation mechanisms and control strategies for crystal polymorph selection.

TL;DR: It is shown that polymorph selection takes place at the earliest stages of structure formation and is based on specific building blocks for each space group, and ways of controlling macromolecular phase transitions are suggested, aiding the development of protein-based drug-delivery systems and macromolescular crystallography.
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Observing classical nucleation theory at work by monitoring phase transitions with molecular precision

TL;DR: The data show that despite having all the characteristics typically associated with rich phase behaviour, glucose isomerase 2D crystals are formed classically, illustrating the resurfacing importance of the classical nucleation theory by re-validating some of the key assumptions that have been recently questioned.
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Do protein crystals nucleate within dense liquid clusters

TL;DR: Observations indicate that the protein-rich clusters are locations for crystal nucleation and that newly nucleated crystals within protein- rich clusters were detected directly.
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Comparison of Different Experimental Techniques for the Measurement of Crystal Growth Kinetics

TL;DR: The relative merits and domains of application of three observation techniques (atomic force microscopy, Michelson interferometry, and laser confocal microscopy with differential interference contrast microscopy) for the investigation of crystal growth kinetics are discussed in the context of protein crystallization.