Improving Protein Crystallization with Reductive Methylation
Author Information
Author(s): Shaw Neil, Cheng Chongyun, Tempel Wolfram, Chang Jessie, Ng Joseph, Wang Xin-Yu, Perrett Sarah, Rose John, Rao Zihe, Wang Bi-Cheng, Liu Zhi-Jie
Primary Institution: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Hypothesis
Can reductive methylation of surface lysines improve the crystallization of a nuclease that has resisted crystallization?
Conclusion
Reductive methylation introduced new cohesive contacts that enabled the crystallization of a previously difficult-to-crystallize protein.
Supporting Evidence
- Reductive methylation introduced 44 new cohesive contacts that improved crystallization.
- The modified protein showed a more compact structure with better solvent exclusion.
- Crystals diffracted to 1.2 Å resolution, indicating high quality.
Takeaway
Scientists found a way to help proteins form crystals by adding small chemical groups to them, making it easier to study their structure.
Methodology
The study involved modifying the nuclease's surface lysines through reductive methylation and then assessing the crystallization outcomes.
Limitations
The study did not compare the modified protein's structure to that of the unmodified protein.
Digital Object Identifier (DOI)
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