Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12.

@article{Wahl2000FlexibilityCD,
  title={Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12.},
  author={Markus C Wahl and Gleb P. Bourenkov and Hans D. Bartunik and Robert Huber},
  journal={The EMBO journal},
  year={2000},
  volume={19 2},
  pages={174-86}
}
Protein L12, the only multicopy component of the ribosome, is presumed to be involved in the binding of translation factors, stimulating factor-dependent GTP hydrolysis. Crystal structures of L12 from Thermotogamaritima have been solved in two space groups by the multiple anomalous dispersion method and refined at 2.4 and 2.0 A resolution. In both crystal forms, an asymmetric unit comprises two full-length L12 molecules and two N-terminal L12 fragments that are associated in a specific, hetero… CONTINUE READING

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The Protein Data Bank: a computer-based archival file for

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