Mechanisms of protein and virus crystal growth: An atomic force microscopy study of Canavalin crystallization
- Lawrence Livermore National Lab., CA (United States)
- California Univ., Riverside, CA (United States). Dept. of Biochemistry
The evolution of surface morphology and step dynamics during growth of single crystals of the protein Canavalin and of the cubic satellite tobacco mosaic virus crystals (STMV) have been investigated by in situ atomic force microscopy. These two crystals were observed to grow by very different mechanisms. Growth of Canavalin occurs on complex vicinal hillocks formed by multiple, independently acting screw dislocations. Small cluster were observed on the terraces. STMV on the other hand, was observed to grow by 2D nucleation of islands. No dislocations were found on the crystal. The results are used to determine the growth mechanisms and estimate fundamental materials parameters. The images also illustrate the important mechanism of defect incorporation and provide insight to the processes that limit the growth rate and uniformity of these crystals.
- Research Organization:
- Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
- Sponsoring Organization:
- USDOE, Washington, DC (United States)
- DOE Contract Number:
- W-7405-ENG-48
- OSTI ID:
- 85918
- Report Number(s):
- UCRL-JC-120183; CONF-9506203-1; ON: DE95014365
- Resource Relation:
- Conference: 6. ICCG, The Hague (Netherlands), 18-23 Jun 1995; Other Information: PBD: 10 Mar 1995
- Country of Publication:
- United States
- Language:
- English
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