Journal article
Static light scattering studies of OmpF porin: Implications for integral membrane protein crystallization
Protein science, v 9(8), pp 1559-1566
Aug 2000
PMID: 10975577
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Abstract
Integral membrane proteins carry out some of the most
important functions of living cells, yet relatively few
details are known about their structures. This is due, in
large part, to the difficulties associated with preparing
membrane protein crystals suitable for X-ray diffraction
analysis. Mechanistic studies of membrane protein crystallization
may provide insights that will aid in determining future
membrane protein structures. Accordingly, the solution
behavior of the bacterial outer membrane protein OmpF porin
was studied by static light scattering under conditions
favorable for crystal growth. The second osmotic virial
coefficient (B22) was found to be a
predictor of the crystallization behavior of porin, as
has previously been found for soluble proteins. Both tetragonal
and trigonal porin crystals were found to form only within
a narrow window of B22 values located
at approximately −0.5 to −2 × 10−4
mol mL g−2, which is similar to the “crystallization
slot” observed for soluble proteins. The B22
behavior of protein-free detergent micelles proved very
similar to that of porin-detergent complexes, suggesting
that the detergent's contribution dominates the behavior
of protein-detergent complexes under crystallizing conditions.
This observation implies that, for any given detergent,
it may be possible to construct membrane protein crystallization
screens of general utility by manipulating the solution
properties so as to drive detergent B22
values into the crystallization slot. Such screens would
limit the screening effort to the detergent systems most
likely to yield crystals, thereby minimizing protein requirements
and improving productivity.
Metrics
Details
- Title
- Static light scattering studies of OmpF porin: Implications for integral membrane protein crystallization
- Creators
- CARL HITSCHERICH - Department of Chemical and Biochemical Engineering, University of Iowa, Iowa City, Iowa 52242JEFFREY KAPLAN - Department of Pharmacology, University of Pennsylvania, Philadelphia, Pennsylvania 19104MARGARET ALLAMAN - Department of Chemical and Biochemical Engineering, University of Iowa, Iowa City, Iowa 52242JOHN WIENCEK - Department of Chemical and Biochemical Engineering, University of Iowa, Iowa City, Iowa 52242PATRICK J LOLL - Department of Pharmacology, University of Pennsylvania, Philadelphia, Pennsylvania 19104
- Publication Details
- Protein science, v 9(8), pp 1559-1566
- Publisher
- Cambridge University Press
- Number of pages
- 8
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000088917400014
- Scopus ID
- 2-s2.0-0033838103
- Other Identifier
- 991014877865904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology