Crystallization and structural studies of components of the protein-synthesizing system from Thermus thermophilus
β Scribed by M. Garber; N. Davydova; I. Eliseikina; N. Fomenkova; O. Gryaznova; I. Gryshkovskaya; N. Nevskaya; S. Nikonov; A. Rak; S. Sedelnikova; A. Serganov; D. Shcherbakov; S. Tishchenko; V. Vysotskaya; J. Zheltonosova; A. Liljas; A. Aevarsson; S. Al-Karadaghi
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 584 KB
- Volume
- 168
- Category
- Article
- ISSN
- 0022-0248
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Crystals have been obtained for recombinant ribosomal protein S8 from Thermus thermophilus produced by Escherichia coli. The protein crystals have been grown in 40 mM potassium phosphate buffer (pH 6.0) in hanging drops equilibrated against saturated ammonium sulfate (unbuffered) with 2-methyl-
The ba 3 cytochrome oxidase from Thermus thermophilus was studied by resonance Raman spectroscopy. The component spectra of both heme groups were determined by using different excitation wavelengths. In the ferric state the heme a 3 group reveals resonance Raman marker bands characteristic for two h