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Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Abstract
This paper reviews the mathematical basis of maximum likelihood. The likelihood function for macromolecular structures is extended to include prior phase information and experimental standard uncertainties. The assumption that different parts of a structure might have different errors is considered. A method for estimating sigma(A) using 'free' reflections is described and its effects analysed. The derived equations have been implemented in the program REFMAC. This has been tested on several proteins at different stages of refinement (bacterial alpha-amylase, cytochrome c', cross-linked insulin and oligopeptide binding protein). The results derived using the maximum-likelihood residual are consistently better than those obtained from least-squares refinement.
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Items 301–304 of 304
Conformational dynamics of the bacterial E3 ligase SspH1
Kennedy, C. R., Esposito, D., Huber, J., House, D., & Rittinger, K. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110671 · Cited by 1
“Models were iteratively improved by manual building in Coot and refined using both REFMAC and Phenix (41–43).”
HSV ‐1 ICP0 dimer domain adopts a novel β‐barrel fold
(2024) · doi:10.1002/prot.26673 · Cited by 1
The phage protein paratox is a multifunctional metabolic regulator of Streptococcus
Muna, T. H., Rutbeek, N. R., Horne, J., Lao, Y. W., Krokhin, O. V., & Prehna, G. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkae1200
Metadata
- Authors
- Murshudov, G. N., Vagin, A. A., & Dodson, E. J.
- Venue
- Acta Crystallographica Section D Biological Crystallography
- Published
- 1997-05-01
- Volume
- 53
- Issue
- 3
- Pages
- 240-255
- ISSN
- 0907-4449 (ISSN-L)
- OpenAlex
- W2038840577
- Cited by
- 14,742
- References
- 0
- FWCI
- 104.57
- Type
- journal article
- Language
- en
- Open access
- closed
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