Several crystal forms of the Bacillus stearothermophilus 50 S ribosomal particles.
نویسندگان
چکیده
منابع مشابه
Approaching the molecular structure of ribosomes.
Fifteen forms of three-dimensional crystals and three forms of two-dimensional sheets from ribosomal particles have been grown. In all cases only biologically active particles could be crystallized, the crystalline material retaining its integrity and biological activity for months. Cryastallographic data have been collected from crystals of 50 S ribosomal subunits, using synchrotron radiation,...
متن کاملThe crystallization of ribosomal proteins from the 50 S subunit of the Escherichia coli and Bacillus stearothermophilus ribosome.
Several individual intact ribosomal proteins purified from bacterial sources under mild conditions have been crystallized. A number of these are suitable candidates for three-dimensional structural studies by x-ray diffraction techniques. Data collection to 3 A resolution for one of these proteins is in progress.
متن کاملCharacterization of single crystals of the large ribosomal particles from Bacillus stearothermophilus.
Single, three-dimensional crystals of the 50 S ribosomal subunit from Bacillus stearothermophilus (strain NCA) have been characterized using a synchrotron X-ray source. The crystals are orthorhombic with unit cell dimensions: a = 350 A, b = 670 A, c = 905 A, and contain at least one 2-fold screw axis. With cooling to -2 degrees C, the large crystals (1.0 mm X 0.2 mm X 0.1 mm) diffract to 15 to ...
متن کاملHeat stabilities of ribosomal subunits and reassociated ribosomes from Bacillus stearothermophilus.
Absorbance-temperature profiles reveal that both the 30S and 50S ribosomal subunits from Bacillus stearothermophilus are more thermostable than the comparable Escherichia coli particles. Thermophile ribosomes formed by the reassociation of subunits do not display functional heat stability.
متن کاملProteins of the Bacillus stearothermophilus ribosome. A low resolution crystal analysis of protein L30.
The 5 A resolution crystal structure analysis of ribosomal protein L30 from Bacillus stearothermophilus is described. The molecule is shown to be compact and extend to about 25-30 A in each dimension.
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ورودعنوان ژورنال:
- FEBS letters
دوره 154 1 شماره
صفحات -
تاریخ انتشار 1983