TY - JOUR
T1 - Ribosomal crystallography
T2 - From poorly diffracting microcrystals to high-resolution structures
AU - Gluehmann, Marco
AU - Zarivach, Raz
AU - Bashan, Anat
AU - Harms, Joerg
AU - Schluenzen, Frank
AU - Bartels, Heike
AU - Agmon, Ilana
AU - Rosenblum, Gabriel
AU - Pioletti, Marta
AU - Auerbach, Tamar
AU - Avila, Horacio
AU - Hansen, Harly A.S.
AU - Franceschi, François
AU - Yonath, Ada
N1 - Funding Information:
We thank J. M. Lehn for indispensable advice, M. Pope for the heavy atom compounds; M. Wilchek, A. Tocilj, and W. Traub for critical discussions; M. Eisenstein and E. Ben-Zeev for assisting with modeling; R. Wimmer for suggesting the radiodurans, and R. Albrecht, W.S. Bennett, H. Burmeister, C. Brune, C. Glotz, G. Goeltz, M. Kessler, M. Laschever, S. Meier, J. Muessig, M. Peretz, C. Stamer, B. Schmidt, A. Sitka, and A. Vieweger for contributing to different stages of these studies. These studies could not be performed without the cooperation of the staff of the synchrotron radiation facilities at EMBL and MPG beam lines at DESY; ID14/2 & ID14/4 at EMBL and ESRF; and ID19/ APS/ANL. Support was provided by the Max Planck Society, the U.S. National Institutes of Health (GM34360), the German Ministry for Science and Technology (Bundesministerium fuÈ r Bildung, Wis-senschaft, Forschung und Technologie Grant 05-641EA), and the Kimmelman Center for Macromolecular Assembly at the Weizmann Institute. A.Y. holds the Martin S. Kimmel Professorial Chair.
PY - 2001/1/1
Y1 - 2001/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0035721775&partnerID=8YFLogxK
U2 - 10.1006/meth.2001.1241
DO - 10.1006/meth.2001.1241
M3 - Article
C2 - 11860283
AN - SCOPUS:0035721775
SN - 1046-2023
VL - 25
SP - 292
EP - 302
JO - Methods
JF - Methods
IS - 3
ER -