Ribosomal crystallography: from poorly diffracting microcrystals to high-resolution structures.
The cellular organelles translating the genetic code into proteins, the ribosomes, are large, asymmetric, flexible, and unstable ribonucleoprotein assemblies, hence they are difficult to crystallize. Despite two decades of intensive effort and thorough searches for suitable sources, so far only three crystal types have yielded high-resolution structures: two large subunits (from an archaean and from a mesophilic eubacterium) and one thermophilic small subunit. These structures have added to our understanding of decoding, have revealed dynamic aspects of the biosynthetic process, and have indicated the strategies adopted by ribosomes for interacting between themselves as well as with inhibitors, factors and substrates.
Gluehmann
M
M
Max Planck Research Unit for Ribosomal Structure, Notkestrasse 85, 22603 Hamburg, Germany.
Zarivach
R
R
Bashan
A
A
Harms
J
J
Schluenzen
F
F
Bartels
H
H
Agmon
I
I
Rosenblum
G
G
Pioletti
M
M
Auerbach
T
T
Avila
H
H
Hansen
H A
HA
Franceschi
F
F
Yonath
A
A
D001105:Archaea / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray / Q000379:methods*; D008854:Microscopy, Electron; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry; D012270:Ribosomes / Q000737:chemistry* / Q000648:ultrastructure*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D012313:RNA