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Phasing the 30S ribosomal subunit structure

Brodersen, D. E. and Clemons, W. M., Jr. and Carter, A. P. and Wimberly, B. T. and Ramakrishnan, V. (2003) Phasing the 30S ribosomal subunit structure. Acta Crystallographica Section D: Biological Crystallography, 59 (11). pp. 2044-2050. ISSN 0907-4449. doi:10.1107/s0907444903017669.

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The methods involved in determining the 850 kDa structure of the 30S ribosomal subunit from Thermus thermophilus were in many ways identical to those that are generally used in standard protein crystallography. This paper reviews and analyses the methods that can be used in phasing such large structures and shows that the anomalous signal collected from heavy-atom compounds bound to the RNA is both necessary and sufficient for ab initio structure determination at high resolution. In addition, measures to counter problems with non-isomorphism and radiation decay are described.

Item Type:Article
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Clemons, W. M., Jr.0000-0002-0021-889X
Additional Information:© 2003 International Union of Crystallography. (Received 28 January 2003; accepted 7 August 2003) The authors would like to thank Dr Raimond Ravelli for continual help optimizing the data-collection protocol at ESRF ID14-4 and P. R. Evans for critical and helpful comments on the manuscript. DEB was funded by a Human Frontier Science Program postdoctoral fellowship.
Funding AgencyGrant Number
Human Frontier Science ProgramUNSPECIFIED
Subject Keywords:ribosomes; phasing; 30S ribosomal subunit; protein translation
Issue or Number:11
Record Number:CaltechAUTHORS:20181030-134119825
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Official Citation:Brodersen, D. E., Clemons, W. M., Carter, A. P., Wimberly, B. T. & Ramakrishnan, V. (2003). Acta Cryst. D59, 2044-2050.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:90516
Deposited By: George Porter
Deposited On:30 Oct 2018 22:52
Last Modified:16 Nov 2021 03:33

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