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Histogram matching as a new density modification technique for phase refinement and extension of protein molecules
Abstract
A new density modification technique - histogram matching - is being developed with encouraging results. Its application to the known structure of pig 2Zn insulin refines the 6500 1.9 Å MIR phases from a mean error of 60° to one of 46°. With these refined phases as a starting point for phase extension to 1.5 Å, the mean error for the final 13 000 phases is 46°. The original 1.9 Å phases continue to refine during the phase extension to a final mean error of 40°. A comparison is made with similar calculations already published.
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Cited by
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Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore
Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., & Gouaux, J. E. (1996) · Science · doi:10.1126/science.274.5294.1859 · Cited by 2,377
Maximum-likelihood density modification
Terwilliger, T. C. (2000) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900005072 · Cited by 1,634
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Metadata
- Authors
- Zhang, K. Y. J., & Main, P.
- Venue
- Acta Crystallographica Section A Foundations of Crystallography
- Published
- 1990-01-01
- Volume
- 46
- Issue
- 1
- Pages
- 41-46
- ISSN
- 0108-7673 (ISSN-L)
- OpenAlex
- W1990724346
- Cited by
- 171
- References
- 0
- FWCI
- 3.15
- Type
- journal article
- Language
- en
- Open access
- closed
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- Zhang, K. Y. J., & Main, P. (1990). Histogram matching as a new density modification technique for phase refinement and extension of protein molecules. Acta Crystallographica Section A Foundations of Crystallography. https://doi.org/10.1107/s0108767389009311
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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