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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Using more than 801 296 small-molecule crystal structures to aid in protein structure refinement and analysis.
Jason C Cole1, Ilenia Giangreco1, Colin R Groom1
1Cambridge Crystallographic Data Centre, 12 Union Road, Cambridge CB2 1EZ, England.
Acta Crystallographica. Section D, Structural Biology
|December 5, 2017
Summary
This addendum acknowledges key contributions to protein structure solution methods. It highlights the use of Cambridge Structural Database data for advancing crystallographic techniques.
Area of Science:
- Crystallography
- Structural Biology
- Biochemistry
Background:
- The development of protein structure solution methods is crucial for understanding biological processes.
- The Cambridge Structural Database (CSD) contains a vast amount of chemical structure information.
- Previous work by Cole et al. (2017) introduced advancements in protein structure determination.
Purpose of the Study:
- To provide an addendum to the Introduction of Cole et al. (2017).
- To recognize the foundational work of Bricogne, Smart, and others.
- To highlight the significance of Cambridge Structural Database data in protein structure solution.
Main Methods:
- Review of historical contributions to crystallographic methods.
- Analysis of the impact of the Cambridge Structural Database on structural biology.
- Integration of prior research findings into the context of Cole et al. (2017).
Main Results:
- Acknowledgement of Bricogne, Smart, and colleagues' pioneering efforts.
- Recognition of the essential role of Cambridge Structural Database data.
- Contextualization of these contributions within the framework of protein structure solution.
Conclusions:
- The development of protein structure solution is a cumulative effort.
- The Cambridge Structural Database has been instrumental in advancing structural biology.
- Proper attribution is essential for scientific progress and historical accuracy.

