Protein Science, volume 31, issue 1, pages 269-282
EFAMIX , a tool to decompose inline chromatography SAXS data from partially overlapping components
Konarev Petr V.
1
,
Graewert Melissa
2
,
Jeffries Cy M.
2
,
Fukuda Masakazu
3
,
Cheremnykh Taisiia A
2
,
Volkov V. S.
1
,
2
Hamburg Outstation European Molecular Biology Laboratory Hamburg Germany
|
3
Formulation Development Department Chugai Pharmaceutical Co., Ltd. Tokyo Japan
|
Publication type: Journal Article
Publication date: 2021-11-22
Journal:
Protein Science
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 8
ISSN: 09618368, 1469896X
DOI:
10.1002/pro.4237
PubMed ID:
34767272
Biochemistry
Molecular Biology
Abstract
Small‐angle X‐ray scattering (SAXS) is an established technique for structural analysis of biological macromolecules in solution. During the last decade, inline chromatography setups coupling SAXS with size exclusion (SEC‐SAXS) or ion exchange (IEC‐SAXS) have become popular in the community. These setups allow one to separate individual components in the sample and to record SAXS data from isolated fractions, which is extremely important for subsequent data interpretation, analysis, and structural modeling. However, in case of partially overlapping elution peaks, inline chromatography SAXS may still yield scattering profiles from mixtures of components. The deconvolution of these scattering data into the individual fractions is nontrivial and potentially ambiguous. We describe a cross‐platform computer program, EFAMIX, for restoring the scattering and concentration profiles of the components based on the evolving factor analysis (EFA). The efficiency of the program is demonstrated in a number of simulated and experimental SEC‐SAXS data sets. Sensitivity and limitations of the method are explored, and its applicability to IEC‐SAXS data is discussed. EFAMIX requires minimal user intervention and is available to academic users through the program package ATSAS as from release 3.1.
Citations by journals
1
2
3
4
5
|
|
Methods in Enzymology
|
Methods in Enzymology
5 publications, 35.71%
|
Acta Crystallographica Section D: Structural Biology
|
Acta Crystallographica Section D: Structural Biology
1 publication, 7.14%
|
Biophysics and Physicobiology
|
Biophysics and Physicobiology
1 publication, 7.14%
|
Frontiers in Nutrition
|
Frontiers in Nutrition
1 publication, 7.14%
|
Molecular Therapy - Nucleic Acids
|
Molecular Therapy - Nucleic Acids
1 publication, 7.14%
|
Physics of Atomic Nuclei
|
Physics of Atomic Nuclei
1 publication, 7.14%
|
ChemBioChem
|
ChemBioChem
1 publication, 7.14%
|
Analytical Biochemistry
|
Analytical Biochemistry
1 publication, 7.14%
|
Crystallography Reports
|
Crystallography Reports
1 publication, 7.14%
|
Protein Science
|
Protein Science
1 publication, 7.14%
|
1
2
3
4
5
|
Citations by publishers
1
2
3
4
5
6
7
|
|
Elsevier
|
Elsevier
7 publications, 50%
|
Pleiades Publishing
|
Pleiades Publishing
2 publications, 14.29%
|
Wiley
|
Wiley
2 publications, 14.29%
|
International Union of Crystallography (IUCr)
|
International Union of Crystallography (IUCr)
1 publication, 7.14%
|
Biophysical Society of Japan
|
Biophysical Society of Japan
1 publication, 7.14%
|
Frontiers Media S.A.
|
Frontiers Media S.A.
1 publication, 7.14%
|
1
2
3
4
5
6
7
|
- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
{"yearsCitations":{"type":"bar","data":{"show":true,"labels":[2022,2023,2024],"ids":[0,0,0],"codes":[0,0,0],"imageUrls":["","",""],"datasets":[{"label":"Citations number","data":[7,6,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6"],"percentage":["50","42.86","7.14"],"barThickness":null}]},"options":{"indexAxis":"x","maintainAspectRatio":true,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":1,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Citations per year","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"journals":{"type":"bar","data":{"show":true,"labels":["Methods in Enzymology","Acta Crystallographica Section D: Structural Biology","Biophysics and Physicobiology","Frontiers in Nutrition","Molecular Therapy - Nucleic Acids","Physics of Atomic Nuclei","ChemBioChem","Analytical Biochemistry","Crystallography Reports","Protein Science"],"ids":[24566,21603,27811,13807,20403,21914,12154,22528,24474,2646],"codes":[0,0,0,0,0,0,0,0,0,0],"imageUrls":["\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/xG3oC19920mmFVqkoVEGKGaMCeoalzyvWxPkVox5_medium.webp","\/storage\/images\/resized\/YEqjK1faRVFLXik2gpsar1M9RjCFKf86fQnaXFyJ_medium.webp","\/storage\/images\/resized\/4QWA67eqfcfyOiA8Wk7YnqroHFqQbTsmDJUYTCTg_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/oZgeErrVFhuDksyqFURLvYS1wtVSBWczh001igGo_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/oZgeErrVFhuDksyqFURLvYS1wtVSBWczh001igGo_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp"],"datasets":[{"label":"","data":[5,1,1,1,1,1,1,1,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":[35.71,7.14,7.14,7.14,7.14,7.14,7.14,7.14,7.14,7.14],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Journals","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"publishers":{"type":"bar","data":{"show":true,"labels":["Elsevier","Pleiades Publishing","Wiley","International Union of Crystallography (IUCr)","Biophysical Society of Japan","Frontiers Media S.A."],"ids":[17,101,11,730,7020,208],"codes":[0,0,0,0,0,0],"imageUrls":["\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/oZgeErrVFhuDksyqFURLvYS1wtVSBWczh001igGo_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/xG3oC19920mmFVqkoVEGKGaMCeoalzyvWxPkVox5_medium.webp","\/storage\/images\/resized\/YEqjK1faRVFLXik2gpsar1M9RjCFKf86fQnaXFyJ_medium.webp","\/storage\/images\/resized\/4QWA67eqfcfyOiA8Wk7YnqroHFqQbTsmDJUYTCTg_medium.webp"],"datasets":[{"label":"","data":[7,2,2,1,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":[50,14.29,14.29,7.14,7.14,7.14],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Publishers","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}}}
Metrics
Cite this
GOST |
RIS |
BibTex |
MLA
Cite this
GOST
Copy
Konarev P. V. et al. EFAMIX , a tool to decompose inline chromatography SAXS data from partially overlapping components // Protein Science. 2021. Vol. 31. No. 1. pp. 269-282.
GOST all authors (up to 50)
Copy
Konarev P. V., Graewert M., Jeffries C. M., Fukuda M., Cheremnykh T. A., Volkov V. S., Svergun D. EFAMIX , a tool to decompose inline chromatography SAXS data from partially overlapping components // Protein Science. 2021. Vol. 31. No. 1. pp. 269-282.
Cite this
RIS
Copy
TY - JOUR
DO - 10.1002/pro.4237
UR - https://doi.org/10.1002%2Fpro.4237
TI - EFAMIX , a tool to decompose inline chromatography SAXS data from partially overlapping components
T2 - Protein Science
AU - Fukuda, Masakazu
AU - Cheremnykh, Taisiia A
AU - Konarev, Petr V.
AU - Jeffries, Cy M.
AU - Volkov, V. S.
AU - Svergun, Dmitri
AU - Graewert, Melissa
PY - 2021
DA - 2021/11/22 00:00:00
PB - Wiley
SP - 269-282
IS - 1
VL - 31
PMID - 34767272
SN - 0961-8368
SN - 1469-896X
ER -
Cite this
BibTex
Copy
@article{2021_Konarev,
author = {Masakazu Fukuda and Taisiia A Cheremnykh and Petr V. Konarev and Cy M. Jeffries and V. S. Volkov and Dmitri Svergun and Melissa Graewert},
title = {EFAMIX , a tool to decompose inline chromatography SAXS data from partially overlapping components},
journal = {Protein Science},
year = {2021},
volume = {31},
publisher = {Wiley},
month = {nov},
url = {https://doi.org/10.1002%2Fpro.4237},
number = {1},
pages = {269--282},
doi = {10.1002/pro.4237}
}
Cite this
MLA
Copy
Konarev, Petr V., et al. “EFAMIX , a tool to decompose inline chromatography SAXS data from partially overlapping components.” Protein Science, vol. 31, no. 1, Nov. 2021, pp. 269-282. https://doi.org/10.1002%2Fpro.4237.