ReviewActa crystallographica. Section D, Biological crystallography2013
Molecular replacement then and now.
Review in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 63 citations in OpenAlex.
- The transformative impact of AI-enabled AlphaFold 3: evolution, current status, and future prospects in structural biology.Frontiers in artificial intelligence · 2026Review
- Kunitz-type trypsin inhibitor from durian (Durio zibethinus) employs a distinct loop for trypsin inhibition.Protein science : a publication of the Protein Society · 2024Article
- AlphaFold two years on: Validation and impact.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Predicted models and CCP4.Acta crystallographica. Section D, Structural biology · 2023Article
- Structural insights into ubiquitin chain cleavage byLife science alliance · 2023Article
- Structural and Biochemical Analyses of the Butanol Dehydrogenase fromInternational journal of molecular sciences · 2023Article
- A general method for directly phasing diffraction data from high-solvent-content protein crystals.IUCrJ · 2022Article
- MrParse: finding homologues in the PDB and the EBI AlphaFold database for molecular replacement and more.Acta crystallographica. Section D, Structural biology · 2022Article
- Modeling a unit cell: crystallographic refinement procedure using the biomolecular MD simulation platformIUCrJ · 2022Article
- Implications of AlphaFold2 for crystallographic phasing by molecular replacement.Acta crystallographica. Section D, Structural biology · 2022Review
- Crystallographic molecular replacement using an in silico-generated search model of SARS-CoV-2 ORF8.Protein science : a publication of the Protein Society · 2021Article
- Article
- High-accuracy protein structures by combining machine-learning with physics-based refinement.Proteins · 2020Article
- Experimental Phasing of MicroED Data Using Radiation Damage.Structure (London, England : 1993) · 2020Article
- MicroED methodology and development.Structural dynamics (Melville, N.Y.) · 2020Article
- Using Phaser and ensembles to improve the performance of SIMBAD.Acta crystallographica. Section D, Structural biology · 2020Article
- BLASTing away preconceptions in crystallization trials.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Ab initio structure solution of a proteolytic fragment using ARCIMBOLDO.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Serial femtosecond crystallography at the SACLA: breakthrough to dynamic structural biology.Biophysical reviews · 2018Review
- From electron crystallography of 2D crystals to MicroED of 3D crystals.Current opinion in colloid & interface science · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The `phase problem' in crystallography results from the inability to directly measure the phases of individual diffracted X-ray waves. While intensities are directly measured during data collection, phases must be obtained by other means. Several phasing methods are available (MIR, SAR, MAD, SAD and MR) and they all rely on the premise that phase information can be obtained if the positions of marker atoms in the unknown crystal structure are known. This paper is dedicated to the most popular phasing method, molecular replacement (MR), and represents a personal overview of the development, use and requirements of the methodology. The first description of noncrystallographic symmetry as a tool for structure determination was explained by Rossmann and Blow [Rossmann & Blow (1962), Acta Cryst. 15, 24-31]. The term `molecular replacement' was introduced as the name of a book in which the early papers were collected and briefly reviewed [Rossmann (1972), The Molecular Replacement Method. New York: Gordon & Breach]. Several programs have evolved from the original concept to allow faster and more sophisticated searches, including six-dimensional searches and brute-force approaches. While careful selection of the resolution range for the search and the quality of the data will greatly influence the outcome, the correct choice of the search model is probably still the main criterion to guarantee success in solving a structure using MR. Two of the main parameters used to define the `best' search model are sequence identity (25% or more) and structural similarity. Another parameter that may often be undervalued is the quality of the probe: there is clearly a relationship between the quality and the correctness of the chosen probe and its usefulness as a search model. Efforts should be made by all structural biologists to ensure that their deposited structures, which are potential search probes for future systems, are of the best possible quality.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.