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The octameric histone core of the nucleosome. Structural issues resolved
Journal of Molecular Biology
|February 11, 1994
Summary
A new crystal structure of the histone octamer reveals its correct dimensions, resolving previous discrepancies. This structural refinement was achieved by re-evaluating heavy-atom positions in the electron density map.
Area of Science:
- Structural Biology
- Crystallography
- Molecular Biology
Background:
- The histone octamer is a fundamental component of chromatin structure.
- Previous low-resolution studies and initial high-resolution attempts yielded conflicting data on its precise dimensions.
Purpose of the Study:
- To accurately determine the crystal structure of the histone octamer at high resolution.
- To resolve discrepancies in reported histone octamer dimensions and reconcile conflicting structural data.
Main Methods:
- X-ray crystallography at 3.1 A resolution.
- Refinement of crystallographic data using identical experimental intensity data as previous studies.
- Re-evaluation and precise determination of heavy-atom site location.
Main Results:
- The histone octamer's crystal structure was determined with a refined R value of 25.5%.
- The overall shape and dimensions of the histone octamer are significantly different from the initially reported model.
- The new dimensions align with previous low-resolution observations.
Conclusions:
- A small shift in heavy-atom site determination led to a misinterpretation of the histone octamer's structure in prior analyses.
- The revised crystal structure provides an accurate representation of the histone octamer's size and shape.
- This study clarifies the structural characteristics of the histone octamer, resolving previous analytical conflicts.