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Updated: Jun 26, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Correlation between protein sequence similarity and x-ray diffraction quality in the protein data bank
Hui-Meng Lu1, Da-Chuan Yin, Ya-Jing Ye
1Institute of Special Environmental Biophysics, Faculty of Life Sciences, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, PR China.
Protein sequence similarity influences X-ray crystallography resolution. Researchers found a correlation between protein sequence similarity and the best resolution achieved, indicating protein structure impacts crystallographic outcomes.
Area of Science:
- Structural Biology
- Biophysics
- Computational Biology
Background:
- X-ray crystallography is the primary method for determining protein 3D structures.
- Obtained resolution is affected by crystal quality, diffraction methods, and X-ray sources.
Purpose of the Study:
- To investigate if protein sequence influences X-ray crystallography resolution.
- To analyze the relationship between sequence similarity and achieved resolution.
Main Methods:
- Extracted protein resolution and sequence data from the Protein Data Bank (PDB).
- Clustered proteins based on sequence similarity.
- Statistically analyzed the correlation between sequence similarity and resolution.
Main Results:
- A significant correlation was observed between protein sequence similarity and the best resolution obtained.
- Protein sequence emerged as a factor affecting crystallographic resolution.
Conclusions:
- Protein structure characteristics, reflected in sequence similarity, play a role in X-ray crystallography resolution.
- This finding adds a new dimension to understanding factors influencing crystallographic outcomes.
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