ArticleJournal of visualized experiments : JoVE2017
Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline.
Article in Journal of visualized experiments : JoVE, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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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Who cites it
22 citing papers in PubMed.
- Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1.Nature communications · 2025Article
- Form factor determination of biological molecules with X-ray free electron laser small-angle scattering (XFEL-SAS).Communications biology · 2023Article
- Upgraded D22 SEC-SANS setup dedicated to the biology community.Journal of applied crystallography · 2023Article
- BioSAXS at European Synchrotron Radiation Facility - Extremely Brilliant Source: BM29 with an upgraded source, detector, robot, sample environment, data collection and analysis software.Journal of synchrotron radiation · 2023Article
- Biochemically validated structural model of the 15-subunit intraflagellar transport complex IFT-B.The EMBO journal · 2022Article
- Molecular architecture of the glycogen- committed PP1/PTG holoenzyme.Nature communications · 2022Article
- Mechanism of CK2 Inhibition by a Ruthenium-Based Polyoxometalate.Frontiers in molecular biosciences · 2022Article
- Structural Analysis of a Genetically Encoded FRET Biosensor by SAXS and MD Simulations.Sensors (Basel, Switzerland) · 2021Article
- Biophysical characterization of the complex between the iron-responsive transcription factor Fep1 and DNA.European biophysics journal : EBJ · 2021Article
- Article
- Structural basis of client specificity in mitochondrial membrane-protein chaperones.Science advances · 2020Article
- Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain.Biophysical journal · 2020Article
- Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.PloS one · 2020Article
- Structural characterization of the third scavenger receptor cysteine-rich domain of murine neurotrypsin.Protein science : a publication of the Protein Society · 2019Article
- Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument.Journal of applied crystallography · 2018Article
- Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.Cell · 2018Article
- Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3.Nature communications · 2018Article
- The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 fromThe Journal of biological chemistry · 2018Article
- Crystal structure of intraflagellar transport protein 80 reveals a homo-dimer required for ciliogenesis.eLife · 2018Article
- Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release.Nature communications · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biological small angle X-ray scattering (BioSAXS) is a powerful technique in molecular and structural biology used to determine solution structure, particle size and shape, and surface-to-volume ratio of macromolecules. The technique is applicable to a very wide variety of solution conditions spanning a broad range of concentrations, pH values, ionic strengths, temperatures, additives, etc., but the sample is required to be monodisperse. This caveat led to the implementation of liquid chromatography systems on SAXS beamlines. Here, we describe the upstream integration of size-exclusion (SEC) and ion-exchange chromatography (IEC) on a beamline, different methods for optimal background subtraction, and data reduction. As an example, we describe how we use SEC- and IEC-SAXS on a fragment of the essential vaccinia virus protein D5, consisting of a D5N helicase domain. We determine its overall shape and molecular weight, showing the hexameric structure of the protein.
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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.