Molecular factors stabilizing protein crystals

F. R. Salemme, Lars Genieser, B. C. Finzel, R. M. Hilmer, J. J. Wendoloski

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


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 languageEnglish (US)
Pages (from-to)273-282
Number of pages10
JournalJournal of Crystal Growth
Issue number1-3
StatePublished - Jul 2 1988
Externally publishedYes


Dive into the research topics of 'Molecular factors stabilizing protein crystals'. Together they form a unique fingerprint.

Cite this