Characterization and crystallization of ribosomal particles from Halobacterium marismortui

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Characterization and crystallization of ribosomal particles from Halobacterium marismortui

Ribosomes and their subunits have been isolated from Halobacterium marismortui, an extremely halophilic bacterium from the Dead Sea. The stability and functional activity of the subunits were tested under a wide range of salt conditions. Three-dimensional microcrystals of the large ribosomal subunits have been obtained. Electron microscopy of positively stained thin sections of these crystals s...

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Crystallization of halophilic malate dehydrogenase from Halobacterium marismortui.

Malate dehydrogenase from the extreme halophile Halobacterium marismortui crystallizes in highly concentrated phosphate solution in space group 12 with cell dimensions a = 113.8 A, b = 122.8 A, c = 126.7 A, beta = 98.1 degrees. The halophilic enzyme was found to be unstable at lower concentrations of phosphate. It associates with unusually large amounts of water and salt, and the combined parti...

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Single crystals of large ribosomal particles from Halobacterium marismortui diffract to 6 A.

Large, well-ordered three-dimensional crystals of 50 S ribosomal subunits from Halobacterium marismortui have been obtained by seeding. The crystals have been characterized with synchrotron X-ray radiation as monoclinic, space group P2(1), with unit cell dimensions of a = 182(+/- 5) A, b = 584(+/- 10) A, c = 186(+/- 5) A, beta = 109 degrees. At 4 degrees C, the crystals (0.6 mm X 0.6 mm X 0.1 m...

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The primary structures of ribosomal proteins S14 and S16 from the archaebacterium Halobacterium marismortui. Comparison with eubacterial and eukaryotic ribosomal proteins.

The amino acid sequences of two ribosomal proteins, S14 and S16, from the archaebacterium Halobacterium marismortui have been determined. Sequence data were obtained by the manual and solid-phase sequencing of peptides derived from enzymatic digestions with trypsin, chymotrypsin, pepsin, and Staphylococcus aureus protease as well as by chemical cleavage with cyanogen bromide. Proteins S14 and S...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1985

ISSN: 0014-5793

DOI: 10.1016/0014-5793(85)80655-4