Published November 2003
| Published
Journal Article
Open
Phasing the 30S ribosomal subunit structure
Chicago
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Abstract
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.
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.Attached Files
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Additional details
- Eprint ID
- 90516
- Resolver ID
- CaltechAUTHORS:20181030-134119825
- Human Frontier Science Program
- Created
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2018-10-30Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field