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

Architectures of Whole-Module and Bimodular Proteins from the 6-Deoxyerythronolide B Synthase

Edwards, A. L., Matsui, T., Weiss, T. M., & Khosla, C. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.03.015 · Cited by 60

ISPyB for BioSAXS, the gateway to user autonomy in solution scattering experiments

Antolinos, A. D. M., Pernot, P., Brennich, M., Kieffer, J., Bowler, M. W., Delageniere, S., Ohlsson, S., Monaco, S., Ashton, A., Franke, D., et al. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004714019609 · Cited by 60

Rifampin phosphotransferase is an unusual antibiotic resistance kinase

Stogios, P. J., Cox, G., Spanogiannopoulos, P., Pillon, M. C., Waglechner, N., Skarina, T., Koteva, K. K., Guarné, A., Savchenko, A. V., & Wright, G. D. (2016) · Nature Communications · doi:10.1038/ncomms11343 · Cited by 61

Transient and stabilized complexes of Nsp7, Nsp8, and Nsp12 in SARS-CoV-2 replication

Wilamowski, M., Hammel, M., Leite, W. C., Zhang, Q., Kim, Y., Weiss, K. L., Jedrzejczak, R. P., Rosenberg, D. J., Fan, Y., Wower, J., et al. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.06.006 · Cited by 60

Structural Analysis of Multi-component Amyloid Systems by Chemometric SAXS Data Decomposition

Herranz-Trillo, F., Groenning, M., van Maarschalkerweerd, A., Tauler, R., Vestergaard, B., & Bernadó, P. (2016) · Structure · doi:10.1016/j.str.2016.10.013 · Cited by 60

Evolution of the Plant Reproduction Master Regulators LFY and the MADS Transcription Factors: The Role of Protein Structure in the Evolutionary Development of the Flower

Silva, C. S., Puranik, S., Round, A. R., Brennich, M., Jourdain, A., Parcy, F., Hugouvieux, V., & Zubieta, C. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2015.01193 · Cited by 58

Mechanistic insights into the role of Hop2-Mnd1 in meiotic homologous DNA pairing

Zhao, W., Saro, D., Hammel, M., Kwon, Y., Xu, Y., Rambo, R. P., Williams, G. J., Chi, P., Lu, L., Pezza, R. J., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt924 · Cited by 57

Structure and regulation of human epithelial cell transforming 2 protein

Chen, M., Pan, H., Sun, L., Shi, P., Zhang, Y., Li, L., Huang, Y., Chen, J., Jiang, P., Fang, X., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1913054117 · Cited by 59

Microchemical Engineering in a 3D Ordered Channel Enhances Electrocatalysis

Chen, Q.-X., Liu, Y., He, Z., Wang, J., Liu, J., Jiang, H., Huang, W., Gao, G., Hou, Z., & Yu, S. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c04653 · Cited by 56

Tankyrase-1 Ankyrin Repeats Form an Adaptable Binding Platform for Targets of ADP-Ribose Modification

Eisemann, T., McCauley, M., Langelier, M.-F., Gupta, K., Roy, S., Duyne, G. D. V., & Pascal, J. M. (2016) · Structure · doi:10.1016/j.str.2016.07.014 · Cited by 56

Structural basis for AcrVA4 inhibition of specific CRISPR-Cas12a

Knott, G. J., Cress, B. F., Liu, J., Thornton, B. W., Lew, R. J., Al-Shayeb, B., Rosenberg, D. J., Hammel, M., Adler, B. A., Lobba, M. J., et al. (2019) · eLife · doi:10.7554/elife.49110 · Cited by 58

Adding Size Exclusion Chromatography (SEC) and Light Scattering (LS) Devices to Obtain High-Quality Small Angle X-Ray Scattering (SAXS) Data

Graewert, M. A., Vela, S. D., Gräwert, T., Molodenskiy, D. S., Blanchet, C. E., Svergun, D. I., & Jeffries, C. M. (2020) · Crystals · doi:10.3390/cryst10110975 · Cited by 56

Loosely-packed dynamical structures with partially-melted surface being the key for thermophilic argonaute proteins achieving high DNA-cleavage activity

Zheng, L., Lu, H. J., Zan, B., Li, S., Liu, H., Liu, Z., Huang, J., Liu, Y., Jiang, F., Liu, Q., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac565 · Cited by 56

Defining NADH-Driven Allostery Regulating Apoptosis-Inducing Factor

Brosey, C. A., Ho, C. M. W., Long, W., Singh, S., Burnett, K. H., Hura, G. L., Nix, J. C., Bowman, G. R., Ellenberger, T., & Tainer, J. A. (2016) · Structure · doi:10.1016/j.str.2016.09.012 · Cited by 55

Mitochondrial Cysteine Desulfurase and ISD11 Coexpressed in Escherichia coli Yield Complex Containing Acyl Carrier Protein

Cai, K., Frederick, R. O., Tonelli, M., & Markley, J. L. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.6b01005 · Cited by 55

Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism

Hadži, S., Garcia‐Pino, A., Haesaerts, S., Jurėnas, D., Gerdes, K., Lah, J., & Loris, R. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx138 · Cited by 54

RNA Modifications: Reversal Mechanisms and Cancer

Thapar, R., Bacolla, A., Oyeniran, C., Brickner, J. R., Chinnam, N. B., Mosammaparast, N., & Tainer, J. A. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00949 · Cited by 54

Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog

Sivá, M., Svoboda, M., Veverka, V., Trempe, J., Hofmann, K., Kožíšek, M., Hexnerova, R., Sedlák, F., Belza, J., Brynda, J., et al. (2016) · Scientific Reports · doi:10.1038/srep30443 · Cited by 53

Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor

Thomsen, N. D., Lawson, M. R., Witkowsky, L. B., Qu, S., & Berger, J. M. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616745113 · Cited by 53

Recent advances in small-angle scattering and its expanding impact in structural biology

Trewhella, J. (2021) · Structure · doi:10.1016/j.str.2021.09.008 · Cited by 52

Huntingtin structure is orchestrated by HAP40 and shows a polyglutamine expansion-specific interaction with exon 1

Harding, R., Deme, J. C., Hevler, J. F., Tamara, S., Lemak, A. S., Cantle, J. P., Szewczyk, M. M., Begeja, N., Goss, S., Zuo, X., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02895-4 · Cited by 56

Reaction hijacking of tyrosine tRNA synthetase as a new whole-of-life-cycle antimalarial strategy

Xie, S. C., Metcalfe, R. D., Dunn, E. A., Morton, C. J., Huang, S., Puhalovich, T., Du, Y., Wittlin, S., Nie, S., Luth, M. R., et al. (2022) · Science · doi:10.1126/science.abn0611 · Cited by 52

Quantifying radiation damage in biomolecular small-angle X-ray scattering

Hopkins, J. B., & Thorne, R. E. (2016) · Journal of Applied Crystallography · doi:10.1107/s1600576716005136 · Cited by 51

Structure and function of the N‐terminal domain of Ralstonia eutropha polyhydroxyalkanoate synthase, and the proposed structure and mechanisms of the whole enzyme

Kim, Y. J., Choi, S. Y., Kim, J., Jin, K. S., Lee, S. Y., & Kim, K. (2016) · Biotechnology Journal · doi:10.1002/biot.201600649 · Cited by 51

Structure and Function of the TIR Domain from the Grape NLR Protein RPV1

Williams, S. J., Yin, L., Foley, G., Casey, L. W., Outram, M. A., Ericsson, D. J., Lu, J., Mikael Bodén, A., Dry, I. B., & Kobe, B. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.01850 · Cited by 51

Structural and functional characterization of the PNKP–XRCC4–LigIV DNA repair complex

Aceytuno, R. D., Piett, C. G., Havali-Shahriari, Z., Edwards, R. A., Rey, M., Ye, R., Javed, F., Fang, S., Mani, R. S., Weinfeld, M., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx275 · Cited by 51

Conformational dynamics of the TTD–PHD histone reader module of the UHRF1 epigenetic regulator reveals multiple histone-binding states, allosteric regulation, and druggability

Houliston, R. S., Lemak, A. S., Iqbal, A., Ivanochko, D., Duan, S., Kaustov, L., Ong, M. S., Fan, L., Senisterra, G. A., Brown, P. J., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.799700 · Cited by 51

Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding

Guo, H., Tsai, C.-L., Terajima, M., Tan, X., Banerjee, P., Miller, M. D., Liu, X., Jiang, Y. L., Byemerwa, J. K., Alvarado, S. K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-02859-z · Cited by 51

OCP–FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria

Sluchanko, N. N., Slonimskiy, Y. B., Shirshin, E. A., Moldenhauer, M., Friedrich, T., & Maksimov, E. G. (2018) · Nature Communications · doi:10.1038/s41467-018-06195-0 · Cited by 51

Integrative Structure Modeling: Overview and Assessment

Braitbard, M., Schneidman‐Duhovny, D., & Kalisman, N. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111429 · Cited by 52

Conserved Outer Tegument Component UL11 from Herpes Simplex Virus 1 Is an Intrinsically Disordered, RNA-Binding Protein

Metrick, C. M., Koenigsberg, A. L., & Heldwein, E. E. Z. (2020) · mBio · doi:10.1128/mbio.00810-20 · Cited by 51

Mechanism of efficient double-strand break repair by a long non-coding RNA

Thapar, R., Wang, J., Hammel, M., Ye, R., Liang, K., Sun, C., Hnízda, A., Liang, S., Maw, S. S., Lee, L., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa784 · Cited by 53

The dynamic duo: Combining NMR and small angle scattering in structural biology

Hennig, J., & Sattler, M. (2014) · Protein Science · doi:10.1002/pro.2467 · Cited by 50

Structural/Functional Properties of Human NFU1, an Intermediate [4Fe-4S] Carrier in Human Mitochondrial Iron-Sulfur Cluster Biogenesis

Cai, K., Liu, G., Frederick, R. O., Xiao, R., Montelione, G. T., & Markley, J. L. (2016) · Structure · doi:10.1016/j.str.2016.08.020 · Cited by 54

Structural basis for the recognition of complex-type N-glycans by Endoglycosidase S

Trastoy, B., Klontz, E. H., Orwenyo, J., Marina, A., Wang, L., Sundberg, E. J., & Guerin, M. E. (2018) · Nature Communications · doi:10.1038/s41467-018-04300-x · Cited by 50

Drastic changes in conformational dynamics of the antiterminator M2-1 regulate transcription efficiency in Pneumovirinae

Leyrat, C., Renner, M., Harlos, K., Huiskonen, J. T., & Grimes, J. M. (2014) · eLife · doi:10.7554/elife.02674 · Cited by 49

Mechanistic insights into enhancement or inhibition of phase separation by different polyubiquitin chains

Dao, T. P., Yang, Y., Presti, M. F., Cosgrove, M. S., Hopkins, J. B., Ma, W., Loh, S. N., & Castañeda, C. A. (2022) · EMBO Reports · doi:10.15252/embr.202255056 · Cited by 48

Solution and Crystallographic Structures of the Central Region of the Phosphoprotein from Human Metapneumovirus

Leyrat, C., Renner, M., Harlos, K., & Grimes, J. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080371 · Cited by 48

Determination of protein oligomeric structure from small‐angle X‐ray scattering

Korasick, D. A., & Tanner, J. J. (2018) · Protein Science · doi:10.1002/pro.3376 · Cited by 48

The sliding clamp tethers the endonuclease domain of MutL to DNA

Pillon, M. C., Babu, V. M. P., Randall, J. R., Cai, J., Simmons, L. A., Sutton, M. D., & Guarné, A. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv918 · Cited by 48

C-terminal region of bacterial Ku controls DNA bridging, DNA threading and recruitment of DNA ligase D for double strand breaks repair

McGovern, S., Baconnais, S., Roblin, P., Nicolas, P., Drevet, P., Simonson, H., Piétrement, O., Charbonnier, J., Cam, É. L., Noirot, P. H., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw149 · Cited by 52

The bacterial antitoxin HipB establishes a ternary complex with operator DNA and phosphorylated toxin HipA to regulate bacterial persistence

Wen, Y., Behiels, E., Félix, J., Elegheert, J., Vergauwen, B., Devreese, B. V., & Savvides, S. N. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku665 · Cited by 49

Deciphering Solution Scattering Data with Experimentally Guided Molecular Dynamics Simulations

Björling, A., Niebling, S., Marcellini, M., van der Spoel, D., & Westenhoff, S. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/ct5009735 · Cited by 47

A key interaction with RPA orients XPA in NER complexes

Topolska‐Woś, A. M., Sugitani, N., Cordoba, J. J., Meur, K. V. L., Meur, R. A. L., Kim, H. S., Yeo, J.-E., Rosenberg, D. J., Hammel, M., Schärer, O. D., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1231 · Cited by 47

NELL2-Robo3 complex structure reveals mechanisms of receptor activation for axon guidance

Pak, J. S., DeLoughery, Z. J., Wang, J., Acharya, N., Park, Y., Jaworski, A., & Özkan, E. (2020) · Nature Communications · doi:10.1038/s41467-020-15211-1 · Cited by 47

Methods for SAXS‐Based Structure Determination of Biomolecular Complexes

Yang, S. (2014) · Advanced Materials · doi:10.1002/adma.201304475 · Cited by 46

Structurally Distinct Ubiquitin- and Sumo-Modified PCNA: Implications for Their Distinct Roles in the DNA Damage Response

Tsutakawa, S. E., Yan, C., Xu, X., Weinacht, C. P., Freudenthal, B., Yang, K., Zhuang, Z., Washington, M. T., Tainer, J. A., & Ivanov, I. N. (2015) · Structure · doi:10.1016/j.str.2015.02.008 · Cited by 46

Designing and defining dynamic protein cage nanoassemblies in solution

Lai, Y.-T., Hura, G. L., Dyer, K. N., Tang, H. Y. H., Tainer, J. A., & Yeates, T. O. (2016) · Science Advances · doi:10.1126/sciadv.1501855 · Cited by 46

Photoactivation of Drosophila melanogaster cryptochrome through sequential conformational transitions

Berntsson, O., Rodriguez, R., Henry, L., Panman, M. R., Hughes, A. J., Einholz, C., Weber, S., Ihalainen, J. A., Henning, R. W., Kosheleva, I., et al. (2019) · Science Advances · doi:10.1126/sciadv.aaw1531 · Cited by 46

Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms

Duarte, D., Lamontanara, A. J., Sala, G. L., Jeong, S., Sohn, Y., Panjkovich, A., Georgeon, S., Kükenshöner, T., Marcaida, M. J., Pojer, F., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16128-5 · Cited by 46

14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains

Pohl, P., Joshi, R., Petrvalská, O., Obšil, T., & Obšilová, V. (2021) · Communications Biology · doi:10.1038/s42003-021-02419-0 · Cited by 46

Structural studies of RNA-protein complexes: A hybrid approach involving hydrodynamics, scattering, and computational methods

Patel, T. R., Chojnowski, G., Astha, A., Koul, A., McKenna, S. A., & Bujnicki, J. M. (2016) · Methods · doi:10.1016/j.ymeth.2016.12.002 · Cited by 45

Modeling Structure and Dynamics of Protein Complexes with SAXS Profiles

Schneidman‐Duhovny, D., & Hammel, M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7759-8_29 · Cited by 45

Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family

Trempe, J., Šašková, K. G., Sivá, M., Ratcliffe, C. D. H., Veverka, V., Hoegl, A., Ménade, M., Feng, X., Shenker, S., Svoboda, M., et al. (2016) · Scientific Reports · doi:10.1038/srep33671 · Cited by 44

Time-Resolved X-Ray Solution Scattering Reveals the Structural Photoactivation of a Light-Oxygen-Voltage Photoreceptor

Berntsson, O., Diensthuber, R. P., Panman, M. R., Björling, A., Hughes, A. J., Henry, L., Niebling, S., Newby, G. E., Liebi, M., Menzel, A., et al. (2017) · Structure · doi:10.1016/j.str.2017.04.006 · Cited by 44

Biochemical and structural analyses reveal that the tumor suppressor neurofibromin (NF1) forms a high-affinity dimer

Sherekar, M., Han, S., Ghirlando, R., Messing, S. A. J., Drew, M. R., Rabara, D., Waybright, T. J., Juneja, P., O’Neill, H., Stanley, C. B., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010934 · Cited by 44

Simultaneous binding of Guidance Cues NET1 and RGM blocks extracellular NEO1 signaling

Robinson, R. A., Griffiths, S. C., van de Haar, L. L., Malinauskas, T., van Battum, E. Y., Zelina, P., Schwab, R. A., Karia, D., Malinauskaitė, L., Brignani, S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.045 · Cited by 44

Conserved Distal Loop Residues in the Hsp104 and ClpB Middle Domain Contact Nucleotide-binding Domain 2 and Enable Hsp70-dependent Protein Disaggregation

DeSantis, M. E., Sweeny, E. A., Snead, D., Leung, E. H., Go, M. S., Gupta, K., Wendler, P., & Shorter, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.520759 · Cited by 43

Stability, structural and functional properties of a monomeric, calcium–loaded adenylate cyclase toxin, CyaA, from Bordetella pertussis

Cannella, S. E., Enguéné, V. Y. N., Davi, M., Malosse, C., Pérez, A. C. S., Chamot‐Rooke, J., Vachette, P., Christiane, D. D., Ladant, D., & Chenal, A. (2017) · Scientific Reports · doi:10.1038/srep42065 · Cited by 43

Grc3 programs the essential endoribonuclease Las1 for specific RNA cleavage

Pillon, M. C., Sobhany, M., Borgnia, M. J., Williams, J. G., & Stanley, R. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1703133114 · Cited by 43

Modular assembly of a protein nanotriangle using orthogonally interacting coiled coils

Park, W. M., Bedewy, M., Berggren, K. K., & Keating, A. E. (2017) · Scientific Reports · doi:10.1038/s41598-017-10918-6 · Cited by 46

Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex

Butt, B. G., Owen, D. J., Jeffries, C. M., Ivanova, L., Hill, C. H., Houghton, J. W., Ahmed, F., Antrobus, R., Svergun, D. I., Welch, J. J., et al. (2020) · eLife · doi:10.7554/elife.53789 · Cited by 43

Mechanism of efficient double-strand break repair by a long non-coding RNA

Thapar, R., Wang, J., Hammel, M., Ye, R., Liang, K., Sun, C., Hnízda, A., Liang, S., Maw, S. S., Lee, L., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1233 · Cited by 42

Determination of the GH3.12 protein conformation through HPLC-integrated SAXS measurements combined with X-ray crystallography

Round, A. R., Brown, E., Marcelin, R., Kapp, U., Westfall, C. S., Jez, J. M., & Zubieta, C. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913019276 · Cited by 42

Intact Functional Fourteen-subunit Respiratory Membrane-bound [NiFe]-Hydrogenase Complex of the Hyperthermophilic Archaeon Pyrococcus furiosus

McTernan, P. M., Chandrayan, S. K., Wu, C.-H., Vaccaro, B. J., Lancaster, W. A., Yang, Q., Fu, D., Hura, G. L., Tainer, J. A., & Adams, M. W. W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.567255 · Cited by 42

Empirical power laws for the radii of gyration of protein oligomers

Tanner, J. J. (2016) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798316013218 · Cited by 42

Biochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro

Yadav, R., Courouble, V. V., Dey, S. K., Harrison, J. J. E. K., Timm, J., Hopkins, J. B., Slack, R. L., Sarafianos, S. G., Ruiz, F. X., Griffin, P. R., et al. (2022) · Science Advances · doi:10.1126/sciadv.add2191 · Cited by 41

RECONSTRUCTION OF SAXS PROFILES FROM PROTEIN STRUCTURES

Putnam, D. K., Lowe, E. W., & Meiler, J. (2013) · Computational and Structural Biotechnology Journal · doi:10.5936/csbj.201308006 · Cited by 41

Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding

Zorzini, V., Buts, L., Schrank, E., Sterckx, Y. G. ‐., Respondek, M., Engelberg–Kulka, H., Loris, R., Zangger, K., & van Nuland, N. A. J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gku1352 · Cited by 41

Disentangling polydispersity in the PCNA−p15PAF complex, a disordered, transient and multivalent macromolecular assembly

Cordeiro, T. N., Chen, P., Biasio, A. D., Sibille, N., Blanco, F. J., Hub, J. S., Crehuet, R., & Bernadó, P. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1183 · Cited by 41

Abundant neuroprotective chaperone Lipocalin-type prostaglandin D synthase (L-PGDS) disassembles the Amyloid-β fibrils

Kannaian, B., Sharma, B., Phillips, M. F., Chowdhury, A., Manimekalai, M. S. S., Adav, S. S., Ng, J. T. Y., Kumar, A., Lim, S., Mu, Y., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-48819-5 · Cited by 41

Crystal and Solution Structure Analysis of FhuD2 from Staphylococcus aureus in Multiple Unliganded Conformations and Bound to Ferrioxamine-B

Podkowa, K. J., Briere, L.-A. K., Heinrichs, D. E., & Shilton, B. H. (2014) · Biochemistry · doi:10.1021/bi401349d · Cited by 40

An intrinsically disordered entropic switch determines allostery in Phd–Doc regulation

García-Pino, A., Gieter, S. D., Talavera, A., Greve, H. D., Efremov, R. G., & Loris, R. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2078 · Cited by 40

Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes

Oerum, S., Roovers, M., Rambo, R. P., Kopec, J., Bailey, H., Fitzpatrick, F., Newman, J. A., Newman, W. G., Amberger, A., Zschocke, J., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001286 · Cited by 40

EpCAM homo-oligomerization is not the basis for its role in cell-cell adhesion

Gaber, A., Kim, S. J., Kaake, R. M., Benčina, M., Krogan, N. J., Šali, A., Pavšič, M., & Lenar≷cic̆, B. (2018) · Scientific Reports · doi:10.1038/s41598-018-31482-7 · Cited by 40

Structural mechanism for modulation of functional amyloid and biofilm formation by Staphylococcal Bap protein switch

Ma, J., Cheng, X. Q., Xu, Z., Zhang, Y., Valle, J., Fan, S., Zuo, X., Lasa, Í., & Fang, X. (2021) · The EMBO Journal · doi:10.15252/embj.2020107500 · Cited by 40

Refining conformational ensembles of flexible proteins against small-angle x-ray scattering data

Pesce, F., & Lindorff‐Larsen, K. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.10.003 · Cited by 40

To Be Fibrils or To Be Nanofilms? Oligomers Are Building Blocks for Fibril and Nanofilm Formation of Fragments of Aβ Peptide

Selivanova, O. M., Surin, A. K., Ryzhykau, Y. L., Glyakina, A. V., Suvorina, M. Y., Kuklin, A. I., Rogachevsky, V. V., & Galzitskaya, O. V. (2018) · Langmuir · doi:10.1021/acs.langmuir.7b03393 · Cited by 40

Inter-α-inhibitor heavy chain-1 has an integrin-like 3D structure mediating immune regulatory activities and matrix stabilization during ovulation

Briggs, D. C., Langford-Smith, A., Birchenough, H. L., Jowitt, T. A., Kielty, C. M., Enghild, J. J., Baldock, C., Milner, C. M., & Day, A. J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011916 · Cited by 40

The PTEN Tumor Suppressor Forms Homodimers in Solution

Heinrich, F., Chakravarthy, S., Nanda, H., Papa, A., Pandolfi, P. P., Ross, A. H., Harishchandra, R. K., Gericke, A., & Lösche, M. (2015) · Structure · doi:10.1016/j.str.2015.07.012 · Cited by 39

Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1

Knott, G. J., Chong, Y. S., Passon, D. M., Liang, X., Deplazes, E., Conte, M. R., Marshall, A. C., Lee, M., Fox, A. H., & Bond, C. S. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1216 · Cited by 38

DNA binding properties of human Cdc45 suggest a function as molecular wedge for DNA unwinding

Szambowska, A., Teßmer, I., Kursula, P., Usskilat, C., Prus, P., Pospiech, H., & Große, F. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1217 · Cited by 38

A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2–ParE2 antitoxin–toxin complex

Sterckx, Y. G. ‐., Jové, T., Shkumatov, A. V., Garcia‐Pino, A., Geerts, L., Kerpel, M. D., Lah, J., Greve, H. D., Melderen, L. V., & Loris, R. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.007 · Cited by 38

Wing phosphorylation is a major functional determinant of the Lrs14‐type biofilm and motility regulator AbfR1 in Sulfolobus acidocaldarius

Li, L., Banerjee, A., Bischof, L. F., Maklad, H. R. M. A., Hoffmann, L., Henche, A., Véliz, F., Bildl, W., Schulte, U., Orell, A., et al. (2017) · Molecular Microbiology · doi:10.1111/mmi.13735 · Cited by 38

Long non‐coding subgenomic flavivirus RNAs have extended 3D structures and are flexible in solution

Zhang, Y., Zhang, Y., Liu, Z., Cheng, M., Ma, J., Wang, Y., Qin, C., & Fang, X. (2019) · EMBO Reports · doi:10.15252/embr.201847016 · Cited by 38

Biochemical and structural analyses reveal that the tumor suppressor neurofibromin (NF1) forms a high-affinity dimer

Sherekar, M., Han, S., Ghirlando, R., Messing, S. A. J., Drew, M. R., Rabara, D., Waybright, T. J., Juneja, P., O’Neill, H., Stanley, C. B., et al. (2020) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)49919-4 · Cited by 38

Size exclusion chromatography coupled small angle X-ray scattering with tandem multiangle light scattering at the SIBYLS beamline

Rosenberg, D. J., Hura, G. L., & Hammel, M. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.031 · Cited by 37

Critical Role of Interdomain Interactions in the Conformational Change and Catalytic Mechanism of Endoplasmic Reticulum Aminopeptidase 1

Stamogiannos, A., Maben, Z., Papakyriakou, A., Mpakali, A., Kokkala, P., Georgiadis, D., Stern, L. J., & Stratikos, E. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b01170 · Cited by 37

Allosteric inhibition of the guanine nucleotide exchange factor DOCK5 by a small molecule

Ferrandez, Y., Zhang, W., Peurois, F., Akendengué, L., Blangy, A., Zeghouf, M., & Cherfils, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-13619-2 · Cited by 37

Design and characterization of mutant and wildtype huntingtin proteins produced from a toolkit of scalable eukaryotic expression systems

Harding, R., Loppnau, P., Ackloo, S. Z., Lemak, A. S., Hutchinson, A., Hunt, B., Holehouse, A. S., Ho, J. C., Fan, L., Toledo, L. M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007204 · Cited by 38

Structural insights into diverse modes of ICAM-1 binding by Plasmodium falciparum -infected erythrocytes

Lennartz, F., Smith, C. L. C., Craig, A. G., & Higgins, M. K. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911900116 · Cited by 37

The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain

Jung, T., Shin, B., Tamò, G. E., Kim, H., Vijayvargia, R., Leitner, A., Marcaida, M. J., Astorga‐Wells, J., Jung, R., Aebersold, R. H., et al. (2020) · Structure · doi:10.1016/j.str.2020.06.008 · Cited by 37

Emerging applications of small angle solution scattering in structural biology

Chaudhuri, B. N. (2014) · Protein Science · doi:10.1002/pro.2624 · Cited by 36

Mechanism of increased clearance of glycated albumin by proximal tubule cells

Wagner, M. C., Myslinski, J., Yadav, S. P. S., Flores, B. N., Rhodes, G. J., Campos, S. B., Sandoval, R. M., Kumar, S., Patel, M., Ashish, et al. (2016) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00605.2015 · Cited by 37

Reciprocal Grids: A Hierarchical Algorithm for Computing Solution X-ray Scattering Curves from Supramolecular Complexes at High Resolution

Ginsburg, A., Ben‐Nun, T., Asor, R., Shemesh, A., Ringel, I., & Raviv, U. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6b00159 · Cited by 36

The Human Centriolar Protein CEP135 Contains a Two-Stranded Coiled-Coil Domain Critical for Microtubule Binding

Kraatz, S. H. W., Guichard, P., Obbineni, J. M., Olieric, N., Hatzopoulos, G. N., Hilbert, M., Sen, I., Missimer, J. H., Gönczy, P., & Steinmetz, M. O. (2016) · Structure · doi:10.1016/j.str.2016.06.011 · Cited by 36

Recent developments in small-angle X-ray scattering and hybrid method approaches for biomacromolecular solutions

Schroer, M. A., & Svergun, D. I. (2018) · Emerging Topics in Life Sciences · doi:10.1042/etls20170138 · Cited by 35

A molecular model for self-assembly of the synaptonemal complex protein SYCE3

Dunne, O. M., & Davies, O. R. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008404 · Cited by 36

Long-range distance determination in fully deuterated RNA with pulsed EPR spectroscopy

Endeward, B., Hu, Y., Bai, G., Liu, G., Prisner, T. F., & Fang, X. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.12.007 · Cited by 35

Anti-PolyQ Antibodies Recognize a Short PolyQ Stretch in Both Normal and Mutant Huntingtin Exon 1

Owens, G. E., New, D. M., West, A. P., & Björkman, P. J. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.05.023 · Cited by 35

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