Halobacterium halobium. I. A thin-sectioning electron-microscopic study.

J D Robertson; W Schreil; M Reedy

doi:10.1016/s0022-5320(82)90014-4

Home/Archive/PubMed

PubMed · 6750146

Halobacterium halobium. I. A thin-sectioning electron-microscopic study.

J D Robertson·W Schreil·M Reedy

View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Bacteriorhodopsins Carotenoids Cell Membrane Cell Wall Cytoplasm Halobacterium Histological Techniques Microscopy, Electron Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

J D Robertson, W Schreil, M Reedy. 1982. Halobacterium halobium. I. A thin-sectioning electron-microscopic study.. https://doi.org/10.1016/s0022-5320(82)90014-4

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2004

Assigning protonation patterns in water networks in bacteriorhodopsin based on computed IR spectra.

Explore the source record for details and available documents.

Bacteriorhodopsins↗

PubMed2004

Role of hydrogen-bond network in energy storage of bacteriorhodopsin's light-driven proton pump revealed by ab initio normal-mode analysis.

Vibrational modes of the hydrogen-bond network in the binding site of bacteriorhodopsin (bR), a protein in halobacteria functioning as a light-driven proton pump, were investigated by an ab initio quantum mechanical/molecular mechanical (QM/MM) method. Normal-mode analysis calculations for O-D and N-D stretching modes of internal water molecules and the Schiff base of the retinal chromophore in the early intermediate state, K, reproduced well experimentally observed vibrational spectra. Supported by agreement with observed spectra, the QM/MM calculation suggests that weakened hydrogen bonds upon photoisomerization of the chromophore are an important means of energy storage in bR.

Bacteriorhodopsins↗

PubMed2004

Physical detwinning of hemihedrally twinned hexagonal crystals of bacteriorhodopsin.

Hexagonal crystals of the membrane protein bacteriorhodopsin of space group P6 3 grown in lipidic cubic phase are twinned hemihedrally. It was shown that slow changes of salt concentration in the mother liquor lead to a split of crystals so that the split parts preserved high diffraction quality. Analysis of diffraction data from split crystals by Yeates statistic and Britton plot showed that the split parts are free of twinning. It is concluded that crystals of bacteriorhodopsin are composed of several macroscopic twinning domains with sizes comparable to the original crystal. The appearance of twinning domains during crystal growth and the mechanism of splitting are discussed.

Bacteriorhodopsins↗