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Malonate: a versatile cryoprotectant and stabilizing solution for salt-grown macromolecular crystals
Todd Holyoak1, Timothy D Fenn, Mark A Wilson
1Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454, USA.
Acta Crystallographica. Section D, Biological Crystallography
|December 4, 2003
Summary
Sodium malonate is presented as a versatile cryoprotectant for protein crystals, enabling cryocooling without damage or ice formation. It also serves as a stabilizing solution for crystal manipulation and derivatization.
Area of Science:
- Crystallography
- Structural Biology
- Biophysics
Background:
- High-quality data collection at synchrotron sources necessitates effective cryoprotectants.
- Protein crystals require cryocooling to prevent radiation damage during data acquisition.
- Ice formation during cryocooling can damage protein crystals, compromising data quality.
Purpose of the Study:
- To introduce sodium malonate as a cryoprotectant for protein crystals.
- To evaluate the efficacy of sodium malonate in preventing ice formation and crystal damage during cryocooling.
- To explore the utility of sodium malonate as a stabilizing solution for crystal manipulation.
Main Methods:
- Cryocooling of protein crystals using sodium malonate solutions.
- Assessment of crystal integrity post-cryocooling.
- Evaluation of sodium malonate's performance as a stabilizing solution for derivatization and ligand soaking.
Main Results:
- Sodium malonate effectively cryoprotects protein crystals, preventing ice formation and damage.
- The compound facilitates manipulation, derivatization, and ligand soaking of salt-grown crystals.
- These processes may not be feasible using the crystal's native mother liquor.
Conclusions:
- Sodium malonate is a versatile cryoprotectant for protein crystallography.
- It offers additional benefits as a stabilizing solution, enhancing experimental possibilities.
- This expands the toolkit for obtaining high-quality diffraction data from challenging crystal systems.