Related Experiment Video
Updated: Feb 21, 2026

11:20
Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology
Published on: January 24, 2018
17.0K
Berkeley Screen: a set of 96 solutions for general macromolecular crystallization
Jose H Pereira1,2, Ryan P McAndrew1,2, Giovani P Tomaleri2
1Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Summary
A new crystallization screen, the Berkeley Screen, was developed using statistical analysis and prior knowledge. This tool aids in protein structure determination and offers an efficient alternative for macromolecular crystallization trials.
Area of Science:
- Structural Biology
- Biochemistry
- Crystallography
Background:
- Protein crystallization is crucial for determining high-resolution structures.
- Understanding the role of crystallization reagents is key to optimizing crystal formation.
- Existing commercial screens may not be universally effective.
Purpose of the Study:
- To develop an efficient and broadly applicable crystallization screen for macromolecules.
- To leverage statistical analysis of existing data to inform screen design.
- To provide a valuable alternative to current commercial crystallization solutions.
Main Methods:
- Statistical analysis of the Biological Macromolecular Crystallization Database.
- Integration of prior knowledge regarding crystallization reagents.
- Correlation of crystallization conditions with high-resolution protein structures.
Main Results:
- Creation of the Berkeley Screen, a novel set of crystallization solutions.
- Identification of key ions and small molecules influencing protein crystal packing.
- Successful application of the Berkeley Screen in crystallizing diverse target proteins.
Conclusions:
- The Berkeley Screen is an effective tool for general macromolecular crystallization.
- The screen has contributed to new Protein Data Bank entries and publications.
- It offers an efficient and valuable alternative for the crystallographic community.

