Better results with homogeneous biological macromolecules
Bernard Lorber (ARN)

TL;DR
This paper emphasizes that using pure and homogeneous biological macromolecules is crucial for obtaining consistent, reliable, and high-quality results in biochemical, biophysical, crystallography, and electron microscopy experiments.
Contribution
It highlights the importance of macromolecular homogeneity for improving experimental reproducibility and data quality in structural biology.
Findings
Homogeneous macromolecules lead to better crystallization and diffraction.
Pure samples improve reproducibility of biochemical measurements.
Homogeneity enhances electron microscopy imaging quality.
Abstract
Pure and homogeneous biological macromolecules (i.e. proteins, nucleic acids, protein-protein or protein-nucleic acid complexes, and functional assemblies such as ribosomes and viruses) are the key for consistent and reliable biochemical and biophysical measurements, as well as for reproducible crystallizations, best crystal diffraction properties, and exploitable electron microscopy images. Highlights: Pure and homogeneous macromolecules are the key for the best experimental results; They warrant the consistency and the reliability of biochemical and biophysical data; They give more reproducible crystallography and electron microscopy results as well.
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Taxonomy
TopicsEnzyme Structure and Function · RNA and protein synthesis mechanisms · Protein Structure and Dynamics
