Abstract：
:In parallel with crystallographic studies of ribosomes from Thermus thermophilus, a long-term program on the crystallization and structural investigations of ribosomal proteins from the same microorganism has been started at the Institute of Protein Research (Pushchino, Russia). At present, more than half of the individual ribosomal proteins from T thermophilus have been purified without denaturating agents on a preparative scale and some of them have been obtained in the crystalline form. X-ray structural analysis of two ribosomal proteins, L1 and S6, is being carried out jointly with the Institute of Molecular Biology (Moscow, Russia) and laboratory of professor A Liljas (Lund University, Sweden). L1 is the large protein of the large ribosomal subunit. It can bind not only to a specific site on the 23S rRNA, but also to the mRNA that codes for L1 and L11, thereby acting as a translational repressor for the synthesis of these proteins. The crystals of L1 are orthorhombic and diffract to about 2 A resolution. Native data and data for several heavy atom derivatives have been collected. S6 is a small acidic protein from the small ribosomal subunit. The crystals of S6 are orthorhombic and diffract to 2 A resolution. Native data and derivatives' data have been collected.
journal_name
Biochimiejournal_title
Biochimieauthors
Garber MB,Agalarov SC,Eliseikina IA,Fomenkova NP,Nikonov SV,Sedelnikova SE,Shikaeva OS,Vasiliev D,Zhdanov AS,Liljas Adoi
10.1016/0300-9084(92)90110-zkeywords:
subject
Has Abstract,Author List Incompletepub_date
1992-04-01 00:00:00pages
327-36issue
4eissn
0300-9084issn
1638-6183pii
0300-9084(92)90110-Zjournal_volume
74pub_type
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