Evidence map›Paper›PMID 34761467›Full record

ArticleProtein science : a publication of the Protein Society2022

SAXSMoW 3.0: New advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale.

Mario de Oliveira Neto, Adriano de Freitas Fernandes, Vassili Piiadov, Aldo Felix Craievich, Evandro Ares de Araújo, Igor Polikarpov

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Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

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0cells of the map it votes in
9citing papers in PubMed
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1 · What the graph read from it

What it found

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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.

2 · The registry

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3 · Its place in the literature

Who cites it

9 citing papers in PubMed.

  1. SASBDB reaches 5000 data sets: empowering open science and next-generation SAS analysis.Acta crystallographica. Section D, Structural biology · 2026
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  2. Review
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  4. Crystal structure of coagulation factor XII N-terminal domains 1-5.Acta crystallographica. Section D, Structural biology · 2025
    Article
  5. Article
  6. Article
  7. Article
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  9. Article
4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Mario de Oliveira NetoBiophysics and Pharmacology Department, Bioscience Institute, Universidade Estadual Paulista, Botucatu, São Paulo, Brazil.
Adriano de Freitas FernandesSao Carlos Institute of Physics, University of Sao Paulo, São Paulo, Brazil.
Vassili PiiadovSao Carlos Institute of Physics, University of Sao Paulo, São Paulo, Brazil.
Aldo Felix CraievichDepartment of Applied Physics, University of Sao Paulo, São Paulo, São Paulo, Brazil.
Evandro Ares de AraújoBrazilian Synchrotron Light Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, São Paulo, Brazil.
Igor PolikarpovSao Carlos Institute of Physics, University of Sao Paulo, São Paulo, Brazil.ORCID 0000-0001-9496-4174

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SAXSMoW (SAXS Molecular Weight) is an online platform widely used over the past few years for determination of molecular weights of proteins in dilute solutions. The scattering intensity retrieved from small-angle X-ray scattering (SAXS) raw data is the sole input to SAXSMoW for determination of molecular weights of proteins in liquid. The current updated SAXSMoW version 3.0 determines the linear dependence of the true protein volume on their apparent protein volume, based on SAXS curves calculated for 67,000 protein structures selected from the Protein Data Bank. SAXSMoW 3.0 was tested against 43 experimental SAXS scattering curves from proteins with known molecular weights. Our results demonstrate that most of the molecular weights determined for the nonglycosylated and also for the glycosylated proteins are in good agreement with their expected molecular weights. Additionally, the average discrepancies between the calculated molecular weights and their nominal values for glycosylated proteins are similar to those for nonglycosylated ones.

Indexed as

Databases, ProteinMolecular Dynamics SimulationScattering, Small AngleSoftwareX-Ray DiffractionMolecular WeightProteinsProteinsmolecular weightprotein densitySAXS

Identifiers

PMID34761467
PMCPMC8740845

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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.