ArticleActa crystallographica. Section A, Foundations and advances2016
Improving the efficiency of molecular replacement by utilizing a new iterative transform phasing algorithm.
Article in Acta crystallographica. Section A, Foundations and advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- CrysFormer: Protein structure determination via Patterson maps, deep learning, and partial structure attention.Structural dynamics (Melville, N.Y.) · 2024Article
- Article
- Inhibition of the Staphylococcus aureus c-di-AMP cyclase DacA by direct interaction with the phosphoglucosamine mutase GlmM.PLoS pathogens · 2019Article
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5 authors.
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Abstract
An iterative transform method proposed previously for direct phasing of high-solvent-content protein crystals is employed for enhancing the molecular-replacement (MR) algorithm in protein crystallography. Target structures that are resistant to conventional MR due to insufficient similarity between the template and target structures might be tractable with this modified phasing method. Trial calculations involving three different structures are described to test and illustrate the methodology. The relationship of the approach to PHENIX Phaser-MR and MR-Rosetta is discussed.
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