Article
Two-dimensional crystallization of Escherichia coli-expressed bacteriorhodopsin and its D96N variant: high resolution structural studies in projection.
Biophysical journal - 1 Sept 1993
Mitra A K, Miercke L J, Turner G J, Shand R F, Betlach M C, Stroud R M
Abstract excerpt
Highly ordered two-dimensional (2-D) crystals of Escherichia coli-expressed bacteriorhodopsin analog (e-bR) and its D96N variant (e-D96N) reconstituted in Halobacterium halobium lipids have been obtained by starting with the opsin protein purified in the denaturing detergent sodium dodecyl sulfat...
Topics
- Bacteriorhodopsins
- Biophysical Phenomena
- Biophysics
- Crystallization
- Crystallography, X-Ray
- Escherichia coli
- Fourier Analysis
- Genetic Variation
- Halobacterium salinarum
- Molecular Structure
- Protein Conformation
- Recombinant Proteins
