With a view to experimental results on protein crystal nucleation the effects of cluster coalescence are probed semi-quantitatively. The steric association restriction, which stems from the patchy surface of the protein molecules, explains both experimentally measured low crystal nucleation rate and coalescence limitations for crystalline clusters of protein molecules. The conclusion is that due to its action, and the impact of rotational diffusion, the coalescence of critical (and/or supercritical) clusters should be rejected as a conceivable alternative for explaining the slow nucleation of protein crystals. Besides, the analysis of cluster-cluster aggregation on diffusional encounters may be of more general interest; it may be helpful by considering the coalescence of structured bio-nano-particles.

---

If you have come directly to this page, click this symbol to go to the CRT homepage.

The full text of this paper in pdf-Format is available at Wiley Interscience for registered users or as "Pay per View".