Abstract
Crystal properties of two proteins, cytochrome ć and hen egg-white lysozyme, are described in a context emphasizing characteristics of molecular structure important in lattice formation and stability. Major factors involved in lattice formation include protein conformational flexibility and incorporation of structured solvent at crystal contacts. Although protein surfaces provide multiple bonding sites, different crystal forms of lysozyme incorporate similar molecular chains. Molecular chain formation in proteins may be related both to crystal nucleation and development of macroscopic crystal habit.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 273-282 |
| Number of pages | 10 |
| Journal | Journal of Crystal Growth |
| Volume | 90 |
| Issue number | 1-3 |
| DOIs | |
| State | Published - Jul 2 1988 |
| Externally published | Yes |