Accurate assessment of mass, models and resolution by small-angle scattering

The Protein Data Bank

Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723

Robust Regression and Outlier Detection

Piepel, G. F., Rousseeuw, P. J., & Leroy, A. M. (1989) · Technometrics · doi:10.2307/1268828 · Cited by 6,183

Robust Regression and Outlier Detection

Rousseeuw, P. J., & Leroy, A. M. (1987) · Wiley Series in Probability and Statistics · doi:10.1002/0471725382 · Cited by 5,609

Small Angle X-ray Scattering

Hart, M., & Deutsch, M. (1983) · Physics Bulletin · doi:10.1088/0031-9112/34/7/032 · Cited by 4,600

Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877

Small-Angle X-Ray Scattering

Bhushan, B. (2016) · Springer eBooks · doi:10.1007/978-94-017-9780-1_101037 · Cited by 3,800

CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates

Svergun, D. I., Barberato, C., & Koch, M. (1995) · Journal of Applied Crystallography · doi:10.1107/s0021889895007047 · Cited by 3,388

Linking Crystallographic Model and Data Quality

Karplus, P. A., & Diederichs, K. (2012) · Science · doi:10.1126/science.1218231 · Cited by 1,781

Light scattering and the absolute characterization of macromolecules

Wyatt, P. J. (1993) · Analytica Chimica Acta · doi:10.1016/0003-2670(93)80373-s · Cited by 1,433

Resolving domain positions of cellobiose dehydrogenase by small angle X‐ray scattering

Motycka, B., Csarman, F., Tscheließnig, R., Hammel, M., & Ludwig, R. (2023) · FEBS Journal · doi:10.1111/febs.16885 · Cited by 3

Probing the oligomeric re-assembling of bacterial fimbriae in vitro: a small-angle X-ray scattering and analytical ultracentrifugation study

Solovyova, A. S., Peters, D. T., Durá, G., Waller, H., Lakey, J. H., & Fulton, D. A. (2021) · European Biophysics Journal · doi:10.1007/s00249-021-01543-3 · Cited by 3

Dynamic structures in DNA damage responses & cancer

Tainer, J. A. (2015) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2015.04.003 · Cited by 3

Pentameric assembly of glycine receptor intracellular domains provides insights into gephyrin clusteringPreprint

Macha, A., Grünewald, N., Havarushka, N., Burdina, N., Toelzer, C., Merkler, Y., Cabrera‐Orefice, A., Brandt, U., Pauly, T. A., Nagel‐Steger, L., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.10.512828 · Cited by 3

Structural investigation of an RNA device that regulates PD-1 expression in mammalian cells

Stagno, J. R., Deme, J. C., Dwivedi, V., Lee, Y.-T., Lee, H. K., Yu, P., Chen, S.-Y., Fan, L., Degenhardt, M. F. D. S., Chari, R., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf156 · Cited by 2

Characterization and structural basis for the brightness of mCLIFY: A novel monomeric and circularly permuted bright yellow fluorescent protein

Shweta, H., Gupta, K., Zhou, Y., Cui, X., Li, S., Lü, Z., Goldman, Y. E., & Dantzig, J. A. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.05.012 · Cited by 2

Crystal structures of PAK2 reveal new insights into its autoinhibitory mechanism

Hu, H., Luo, Z., Zhang, Y., Fang, X., Zhu, Z., Wu, J., & Wang, Z. (2025) · Structure · doi:10.1016/j.str.2025.07.008 · Cited by 2

Molecular tuning of DNA framework–programmed silicification by cationic silica cluster attachment

Jing, X., Wang, H., Huang, J., Liu, Y., Li, Z., Chen, J., Xu, Y., Li, L., Lin, Y., Buratto, D., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2529275123 · Cited by 2

BilboMD: a web-accessible SAXS and AlphaFold-guided modeling pipeline

Classen, S., Mundo, J. T. D., Kulkarni, D. D., Prabhakar, S., Hicks, A., & Hammel, M. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag377 · Cited by 3

The Rho guanine-nucleotide exchange factor P-Rex2 exhibits structural and regulatory features distinct from the related RhoGEF P-Rex1

Anderson, L. K., Marde, R., Muma, G., Nayak, V., Phan, C., Li, S., & Cash, J. N. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113229 · Cited by 2

Estimation of the molecular weight of nanoparticles using a single small-angle X-ray scattering measurement on a relative scale

Zhigunov, A., & Pleštil, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-87133-x · Cited by 2

Quality of protein structural data and radiation damage estimation at beamline 1.3W: SAXS/WAXS

Kamonsutthipaijit, N., Yutaekool, N., Soontranon, S., & Rugmai, S. (2022) · ScienceAsia · doi:10.2306/scienceasia1513-1874.2022.064 · Cited by 2

Crystal structure and solution state of the C-terminal head region of the narmovirus receptor binding protein

Stelfox, A. J., Oguntuyo, K. Y., Rissanen, I., Harlos, K., Rambo, R. P., Lee, B., & Bowden, T. A. (2023) · mBio · doi:10.1128/mbio.01391-23 · Cited by 2

Thin Film Formation of HSA in the Presence of CTAB-Capped Gold Nanorods through Phase Separation

Halder, K., Sabnam, K., Das, A., Goswami, D. K., & Dasgupta, S. (2024) · Langmuir · doi:10.1021/acs.langmuir.4c00694 · Cited by 2

Structural insights into the enzymatic breakdown of azomycin-derived antibiotics by 2-nitroimdazole hydrolase (NnhA)

Ahmed, F. H., Liu, J., Royan, S., Warden, A. C., Esquirol, L., Pandey, G., Newman, J. M., Scott, C. S., & Peat, T. S. (2024) · Communications Biology · doi:10.1038/s42003-024-07336-6 · Cited by 2

Structural Studies of a Double-Stranded RNA from Trypanosome RNA Editing by Small-Angle X-Ray Scattering

Criswell, A. R., & Mooers, B. H. M. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-1896-6_13 · Cited by 2

SAXS Analysis and Characterization of Anticancer Activity of PNP-UDP Family Protein from Putranjiva roxburghii

Verma, P., Varshney, R., Yadav, S. P. S., Kar, B., Roy, P., & Sharma, A. K. (2022) · The Protein Journal · doi:10.1007/s10930-022-10060-x · Cited by 2

Structure–Activity Relationship of the Dimeric and Oligomeric Forms of a Cytotoxic Biotherapeutic Based on Diphtheria Toxin

Mielecki, M., Ziemniak, M., Ozga, M., Borowski, R., Antosik, J., Kaczyńska, A., & Pająk, B. (2022) · Biomolecules · doi:10.3390/biom12081111 · Cited by 2

From dilute to concentrated solutions of intrinsically disordered proteins: Interpretation and analysis of collected data

Lenton, S., Fagerberg, E., Tully, M. D., & Skepö, M. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.09.021 · Cited by 2

Structural insights on the nucleoprotein C-terminal domain of Měnglà virus

Ferrero, D. S., Gilabert, O. T., & Verdaguer, N. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.02373-23 · Cited by 2

Quantitative selection of sample structures in small-angle scattering using Bayesian methods

Hayashi, Y., Katakami, S., Kuwamoto, S., Nagata, K., Mizumaki, M., & Okada, M. (2024) · Journal of Applied Crystallography · doi:10.1107/s1600576724004138 · Cited by 2

A new algorithm for the reconstruction of protein molecular envelopes from X-ray solution scattering data

Badger, J. (2019) · Journal of Applied Crystallography · doi:10.1107/s1600576719009774 · Cited by 2

Synchrotron Small-Angle X-Ray Scattering on Biological Macromolecules in Solution

Franke, D., & Svergun, D. I. (2015) · Springer eBooks · doi:10.1007/978-3-319-04507-8_34-1 · Cited by 2

Protein Structure and Folding

Cole, L. B., & Kramer, P. R. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-803699-0.00020-7 · Cited by 2

Coil-to-Helix Transition at the Nup358-BicD2 Interface Activates BicD2 for Dynein RecruitmentPreprint

Gibson, J. M., Cui, H., Ali, M. Y., Zhao, X., Debler, E., Zhao, J., Trybus, K. M., Solmaz, S. R., & Wang, C. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.06.443034 · Cited by 2

A large disordered region confers a wide spanning volume to vertebrate Suppressor of Fused as shown in a trans-species solution study

Makamte, S., Thureau, A., Jabrani, A., Paquelin, A., Plessis, A., Sanial, M., Rudenko, O., Oteri, F., Baaden, M., & Biou, V. (2022) · Journal of Structural Biology · doi:10.1016/j.jsb.2022.107853 · Cited by 1

Size and Shape of Primary (Bio)Polyelectrolyte Complexes Chitosan/Gelatin: Study Using Small-Angle X-Ray Scattering from Synchrotron Radiation

Валерьевич, П. А., Litvinov, M. Y., Aleksandr, K., & Danilova, K. (2025) · Polymers · doi:10.3390/polym17091236 · Cited by 1

Detergent Choice Shapes the Solution Structures of Photosystems I and II: Implications for Crystallization and High-Resolution Studies

Golub, M., Boyka, J., Gätcke, J., Hart, O., Haupt, S., Wieland, D. C. F., Blanchet, C. E., Zouni, A., & Pieper, J. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c00767 · Cited by 1

X-ray structure of the metastable SEPT14–SEPT7 coiled coil reveals a hendecad region crucial for heterodimerization

Cavini, Í. A., Winter, A. J., Pereira, H. D., Woolfson, D. N., Crump, M. P., & Garratt, R. C. (2023) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798323006514 · Cited by 1

Structural basis for control of integrative and conjugative element excision and transfer by the oligomeric winged helix–turn–helix protein RdfS

Verdonk, C. J., Agostino, M., Eto, K. Y., Hall, D. A., Bond, C. S., & Ramsay, J. P. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf249 · Cited by 1

Specific phosphoinositide interaction of Jps1 is a key feature during unconventional secretion in Ustilago maydis

Dali, S., Schultz, M., Köster, M., Kamel, M., Busch, M., Steinchen, W., Hänsch, S., Papadopoulos, A., Reiners, J., Smits, S. H. J., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110215 · Cited by 1

Architecture of Pseudomonas aeruginosa glutamyl-tRNA synthetase defines a subfamily of dimeric class Ib aminoacyl-tRNA synthetases

Fenwick, M. K., Mayclin, S. J., Seibold, S. A., DeRocher, A. E., Subramanian, S., Phan, I. Q., Dranow, D. M., Lorimer, D. D., Abramov, A., Choi, R., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2504757122 · Cited by 1

The Paulinella chromatophore transit peptide part2 adopts a structural fold similar to the γ-glutamyl-cyclotransferase fold

Klimenko, V., Reiners, J., Applegate, V. M., Reimann, K., Popowicz, G. M., Hoeppner, A., Papadopoulos, A., Smits, S. H. J., & Nowack, E. C. M. (2025) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiaf504 · Cited by 1

Monitoring Enzyme Clustering in a Highly Crystalline Metal–Organic Framework by Small‐Angle Neutron Scattering

Wang, X., He, L., Qian, S., Su, S., Farha, O. K., & Ma, S. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202522967 · Cited by 1

Disordered N‐termini enhance the thermostability of SGNH ‐hydrolase family polyesterases

Ahmed, F. H., Esquirol, L., Royan, S., Birgan, M. M., French, N. G., Newton, S., Caputo, A. T., & Scott, C. S. (2025) · Protein Science · doi:10.1002/pro.70402 · Cited by 1

Phosphoregulation of RAD51AP1 function in homology-directed repair

Sharma, N., Uhrig, M. E., Kwon, Y., Sung, P., & Wiese, C. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111149 · Cited by 1

EEPD1 evolved a unique DNA clamping dimer protecting reversed replication forks

Shen, R., Sarker, A. H., Chen, Y., Liu, M., Roy, S., Arvai, A. S., Bacolla, A., Ahmed, Z., Katsonis, P., Hammel, M., et al. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag188 · Cited by 1

Solution characterization of TraW, a regulatory protein of the F plasmid type 4 secretion system

Rodriguez, C., & Audette, G. F. (2026) · Structural Dynamics · doi:10.1063/4.0001201 · Cited by 1

Structure of a stand-alone homodimeric nonribosomal peptide synthetase condensation domain reveals occlusion of the canonical carrier-protein interface

Singh, J., Grant, T. D., & Gulick, A. M. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113208 · Cited by 1

Shannon sampling based approach for the structural solution of nano-objects by laboratory and synchrotron SAXS data

De, L., Alberga, D., Scattarella, F., Sibillano, T., Mangini, V., Zhou, B., Stoll, T., & Giannini, C. (2026) · Journal of Applied Crystallography · doi:10.1107/s1600576726004358 · Cited by 1

Structure of the Beat–Side complex reveals their interaction is required for neuromuscular system wiring

Priest, J. M., Zhang, R., Olechwier, A. M., Caspi-Lebovic, A. B., Łukaszczyk, W., Ashley, J., Aher, V., Carrillo, R. A., & Özkan, E. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117661 · Cited by 1

112 Structurally distinct ubiquitin- and SUMO-modified PCNA: implications for their distinct roles in the DNA damage response

Tsutakawa, S. E., Yan, C., Xu, X., Zhuang, Z., Washington, M. T., Tainer, J. A., & Ivanov, I. N. (2015) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2015.1032745 · Cited by 1

Implicit vs. Explicit Solvent Models for Calculating X‐ray Solution Scattering Curves#

Ganesan, P., Kim, J. G., Lee, J. H., Kim, J., & Ihee, H. (2015) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.10178 · Cited by 1

Cofactor-Dependent Structural and Binding Properties of Yeast Cytochrome c Peroxidase

Sterckx, Y. G. ‐., & Volkov, A. N. (2014) · Biochemistry · doi:10.1021/bi500603w · Cited by 1

Reduction of small-angle scattering profiles to finite sets of structural invariants

Houdayer, J., & Poitevin, F. (2017) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s205327331700451x · Cited by 1

Structural studies on Mycobacterium tuberculosis HddA enzyme using small angle X-ray scattering and dynamics simulation techniques

Karan, S., Behl, A., Sagar, A., Bandyopadhyay, A., & Saxena, A. K. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.12.191 · Cited by 1

Examining Membrane Proteins by Neutron Scattering

Ebel, C., Breyton, C., & Martel, A. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0724-4_7 · Cited by 1

SAS, refined

Breidenbach, M. A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2634 · Cited by 1

From dilute to concentrated solutions of intrinsically disordered proteins: Sample preparation and data collection

Lenton, S., Tully, M. D., & Skepö, M. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.036 · Cited by 1

Structural characterization of protein–DNA complexes using small angle X-ray scattering (SAXS) with contrast variation

Hutin, S., Guillotin, A., Zubieta, C., & Tully, M. D. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.021 · Cited by 1

Radioprotective Protein of Tardigrades Dsup (Damage Suppressor) is Resistant to High Doses of Ionizing Radiation

Zarubin, M. P., Nizamieva, A. F., Alexeev, S. I., Mitrofanov, S. V., Gorshkova, Y. E., & Kravchenko, E. (2024) · Moscow University Physics Bulletin · doi:10.3103/s0027134924700024 · Cited by 1

Structural insights into the disulfide isomerase and chaperone activity of TrbB of the F plasmid type IV secretion system

Apostol, A. J., Bragagnolo, N., Rodriguez, C. S., & Audette, G. F. (2024) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2024.100156 · Cited by 1

Structural definition of pseudorabies virus dUTPase reveals a novel folding dimer in the herpesvirus family

Li, J., Ma, S., Yang, R., Xu, J., Wang, Y., & Ye, S. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135696 · Cited by 1

Frataxin Traps Low Abundance Quaternary Structure to Stimulate Human Fe–S Cluster Biosynthesis

Cory, S. A., Lin, C.-W., Patra, S., Havens, S. M., Putnam, C. D., Shirzadeh, M., Russell, D. H., & Barondeau, D. P. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00733 · Cited by 1

Small-Angle Scattering Technique

Anitas, E. M. (2019) · SpringerBriefs in physics · doi:10.1007/978-3-030-26612-7_3 · Cited by 1

Quantifying Concentration Fluctuations in Binary Glass-Forming Systems by Small- and Wide-Angle X-ray Scattering

Jin, X., Zhang, Y., Wang, J., Huo, J., & Wang, L. (2022) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.2c00011 · Cited by 1

Disentangling polydisperse biomolecular systems by Chemometrics decomposition of SAS data

Sagar, A., & Bernadó, P. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.038 · Cited by 1

Protein fibrillation from another small angle—SAXS data analysis of developing systems

Langkilde, A. E., & Vestergaard, B. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.09.025 · Cited by 1

Extracting structural insights from soft X-ray scattering of biological assemblies

Rongpipi, S., Mundo, J. T. D., Gomez, E. D., & Gomez, E. W. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.09.017 · Cited by 2

Biochemical and Biophysical Characterization of Huntingtin

Owens, G. E. (2016) · CaltechTHESIS (California Institute of Technology) · doi:10.7907/z9tm7835 · Cited by 1

Integrative SAXS ‐Driven Computational Modeling of Biomolecular Complexes

Song, L., Lu, L., Huang, W., Ravikumar, K. M., Meng, J., & Yang, S. (2018) · Wiley eBooks · doi:10.1002/9783527697106.ch17 · Cited by 1

Molecular Mechanism of the Strong Cell-Adhesion by Cadherin-23Preprint

Singaraju, G. S., Sagar, A., Kumar, A., Samuel, J. S., Hazra, J. P., Sannigrahi, M. K., Yennamalli, R. M., & Rakshit, S. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3155734 · Cited by 1

Obtaining tertiary protein structures by the ab-initio interpretation of small angle X-ray scattering dataPreprint

Prior, C. B., Davies, O. R., Bruce, D., & Pohl, E. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/572057 · Cited by 1

Structural plasticity of 2A proteins in the Parechovirus familyPreprint

Zhu, L., Pichon, M., Pietras, Z., Wang, X., Ren, J., Fry, E. E., Stuart, D. I., Anastassis Perrakis, A., & von Castelmur, E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.06.588386 · Cited by 1

Structural and Functional Characterization of Encapsulin-Targeted Double Ferritin Fold FerroxidasesPreprint

Anuchina, A. A., Remeeva, A., Natarov, I., Yudenko, A., Ebrahim, R. A., Shishkin, P., Sudarev, V. V., Matveeva, V. O., Semenov, O., Kuznetsova, E., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.13.676036 · Cited by 1

DNA binding drives phase separation of the Gcn4 bZIP domain and reveals its conformational ensemble in the diluted and condensate phasesPreprint

Caliò, A., Turbant, F., Tully, M. D., Sharma, S., Schifino, G., Parracino, A., Peters, J., & Pastore, A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.10.704833 · Cited by 1

Biochemical and structural study of MARS complexes from plasmodium

Ponce, J. R. J. (2020) · theses.fr (ABES) · doi:10.70675/d99d421ezee83z4eeaz88efze0862b93839d · Cited by 1

Correlation of thermostability and conformational changes of catechol 2, 3-dioxygenases from two disparate micro-organisms

Sokolova, A. V., Huang, S., Duff, A. P., Gilbert, E. P., & Li, W. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.07.012

BCL::SAS - Small Angle X-ray / Neutron Scattering Profiles to Assist Protein Structure Prediction

Putnam, D. K. (2016)

Understanding substrate binding and movement in proline catabolic enzymes||Understanding substrate binding and movement in proline catabolic enzymes

Pemberton, T. A. (2014) · doi:10.32469/10355/44498

Solution structure of human STARD1 protein and its interaction with fluorescently-labeled cholesterol analogues with different position of the NBD-groupPreprint

Tugaeva, K. V., Faletrov, Y. V., Allakhverdiev, E. S., Maksimov, E. G., & Sluchanko, N. N. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/116368

Nonstructural 5A (NS5A) protein of hepatitis C virus : self-association, membrane anchoring and interactions with antivirals

Beldar, S. (2017) · doi:10.32657/10356/72671

Structural and mechanistic insights into Mycothiol disulfide reductase, Mycoredoxin-1 and peroxiredoxin alkyl hydroperoxidase subunit E of Mycobacterium tuberculosis

Kumar, A. (2017) · doi:10.32657/10356/72805

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Lo, Y., Pillon, M. C., & Stanley, R. E. (2018) · Journal of Visualized Experiments · doi:10.3791/56953

Biological Small-Angle X-Ray Scattering (SAXS)

Klumpler, T. (2018) · Springer eBooks · doi:10.1007/978-3-319-91352-0_14

Small-Angle X-Ray Scattering for the Study of Proteins in the Ubiquitin Pathway

Trempe, J., & Gehring, K. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8706-1_13

Determinação da estrutura e do estado oligomérico de proteínas chaperonas por espalhamento de raios-x a baixos ângulos (SAXS)

Rodrigues, L. F. D. C. (2020) · doi:10.11606/d.43.2020.tde-24032020-120700

Structural and mechanistic insights into the Rel protein of Mycobacterium tuberculosis

Singal, B. (2020) · doi:10.32657/10356/142669

Integrative Structural Biology: Using X-ray Crystallography, Small-Angle X-ray Scattering, and Cryogenic Electron Microscopy to Determine Protein Structures

Wallen, J. R. (2020) · ACS symposium series · doi:10.1021/bk-2020-1357.ch003

STRUCTURAL STUDIES OF TUBULIN MODIFYING ENZYMES

Adamopoulos, A. (2021) · doi:10.33540/290

Molecular basis of amyloid-β chaperone activity of lipocalin-type prostaglandin D synthase (L-PGDS)

Kannaian, B. (2019) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/137482

An objective metric to guide background correction and interpretation of small-angle X-ray scattering data

Gao, Y., Stachowski, T. R., Snell, E. H., Grant, T. D., & Pearson, A. R. (2021) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s0108767321094782

Synchrotron Small-Angle X-Ray Scattering on Biological Macromolecules in Solution

Franke, D., & Svergun, D. I. (2016) · Springer eBooks · doi:10.1007/978-3-319-14394-1_34

Faculty Opinions recommendation of An unusual topological structure of the HIV-1 Rev response element.

Tang, R. S. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718685106.793486099

VSAS: A smart small-angle scattering data processing tool

Shi, S., Zhong, S., Lu, J., Tang, Y., & Lin, H. (2022) · Nuclear Analysis · doi:10.1016/j.nucana.2022.100012

Full-Length Structure of the Host Targeted Bacterial Effector Bep1 Reveals a Novel Structural Domain Conserved in FIC Effector Proteins From BartonellaPreprint

Huber, M., Wagner, A., Reiners, J., Seyfert, C. E. M., Sharpe, T., Smits, S. H. J., Schirmer, T., & Dehio, C. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4109528

Computational methods for the analysis of solution small-angle X-ray scattering of biomolecules: ATSAS

Mertens, H. D. T. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.09.019

Structure of Helicobacter pylori dihydroneopterin aldolase suggests a fragment-based strategy for isozyme-specific inhibitor design

Shaw, G. X., Fan, L., Cherry, S., Shi, G., Tropea, J. E., & Ji, X. (2023) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2023.100095

Insights into dynamic changes in ADC-7 and P99 cephalosporinases using small angle x-ray scattering (SAXS)

Kumar, I., Sagar, A., Dhiman, K., Bethel, C. R., Hujer, A. M., Carifi, J., Ashish, & Bonomo, R. A. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2240427

Crystal structure of domain of unknown function 507 (DUF507) reveals a new protein fold

McKay, C., Cheng, J., & Tanner, J. J. (2023) · Scientific Reports · doi:10.1038/s41598-023-40558-y

Structural analysis and functional evaluation of the disordered ß–hexosyltransferase region from Hamamotoa (Sporobolomyces) singularis

Dagher, S. F., Vaishnav, A., Stanley, C. B., Meilleur, F., Edwards, B. F. P., & Bruno-Bárcena, J. M. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1291245

Disordered regions and folded modules in CAF-1 promote histone deposition in S. pombePreprint

Ouasti, F., Audin, M., Fréon, K., Quivy, J., Tachekort, M., Cesard, E., Thureau, A., Ropars, V., Varela, P. F., Moal, G., et al. (2024) · eLife · doi:10.7554/elife.91461.2

Reviewer #1 (Public Review): Disordered regions and folded modules in CAF-1 promote histone deposition in S. pombe

(2024) · eLife · doi:10.7554/elife.91461.2.sa2

Reviewer #2 (Public Review): Disordered regions and folded modules in CAF-1 promote histone deposition in S. pombe

Ouasti, F., Audin, M., Fréon, K., et al. (2024) · eLife · doi:10.7554/elife.91461.2.sa1

RADIOPROTECTIVE PROTEIN OF TARDIGRADE DSUP (DAMAGE SUPPRESSOR) IS RESISTANT TO HIGH DOSES OF IONIZING RADIATION

Zarubin, M. P., Nizamieva, A. F., Alexeev, S. I., Mitrofanov, S. V., Gorshkova, Y. E., & Kravchenko, E. (2024) · Vestnik Moskovskogo Universiteta Seriya 3 Fizika Astronomiya · doi:10.55959/msu0579-9392.79.2410702

Full-length structure of the host targeted bacterial effector Bep1 reveals a novel structural domain conserved in FIC effector proteins from BartonellaPreprint

Huber, M., Wagner, A., Reiners, J., Seyfert, C. E., Sharpe, T., Smits, S. H. J., Schirmer, T., & Dehio, C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.25.586700

Structure analysis of the telomere resolvase from the Lyme disease spirochete Borrelia garinii reveals functional divergence of its C-terminal domain

Semper, C., Watanabe, N., Karimullina, E. M., Patel, D. T., Leo, R. D., Castellanos, M., Patel, D., Chaconas, G., & Savchenko, A. V. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae580

Divinylazobenzene-Q-Cage Silyloxy-Silsesquioxane-Based Reversible Photoactuatable Network Polymer Sponges

Sims, C. B., Chandler, E. T., Armenta, H. E., Jazi, M. E., Deller, A. C., & Furgal, J. C. (2026) · Macromolecules · doi:10.1021/acs.macromol.5c03635

Structural and functional studies of the EGF20-27 region reveal new features of the human Notch receptor important for optimal activation

Bo, Z., Rowntree, T. J. W., Johnson, S., Nurmahdi, H., Suckling, R. J., Hill, J. C., Korona, B., Weisshuhn, P. C., Sheppard, D., Meng, Y., et al. (2024) · Structure · doi:10.1016/j.str.2024.10.012

A Macrocycle-Mediated Protein Cage

Flood, R. J., Thureau, A., & Crowley, P. B. (2024) · ACS Macro Letters · doi:10.1021/acsmacrolett.4c00656

SAS, refined

Breidenbach, M. A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2634 · Cited by 1

Resolution and validation of SAS-based structural models

Tuukkanen, A. T., Kleywegt, G. J., & Svergun, D. I. (2017) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s2053273317089161

Resolution ofab initioshapes determined from small-angle scattering

Tuukkanen, A. T., Kleywegt, G. J., & Svergun, D. I. (2016) · IUCrJ · doi:10.1107/s2052252516016018 · Cited by 91

Quality control of protein standards for molecular mass determinations by SAXS

Akiyama, S. (2011) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767311099053

Joint use of SAXS and SANS with high-resolution methods for macromolecular solutions

Svergun, D. I. (2008) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767308097080