Current Research in Structural Biology最新文献

{"title":"Structural insights into the disulfide isomerase and chaperone activity of TrbB of the F plasmid type IV secretion system","authors":"Arnold J. Apostol ,&nbsp;Nicholas J. Bragagnolo ,&nbsp;Christina S. Rodriguez ,&nbsp;Gerald F. Audette","doi":"10.1016/j.crstbi.2024.100156","DOIUrl":"10.1016/j.crstbi.2024.100156","url":null,"abstract":"<div><p>Bacteria have evolved elaborate mechanisms to thrive in stressful environments. F-like plasmids in gram-negative bacteria encode for a multi-protein Type IV Secretion System (T4SS_F) that is functional for bacterial proliferation and adaptation through the process of conjugation. The periplasmic protein TrbB is believed to have a stabilizing chaperone role in the T4SS_F assembly, with TrbB exhibiting disulfide isomerase (DI) activity. In the current report, we demonstrate that the deletion of the disordered N-terminus of TrbB_WT, resulting in a truncation construct TrbB_37-161, does not affect its catalytic <em>in vitro</em> activity compared to the wild-type protein (p = 0.76). Residues W37–K161, which include the active thioredoxin motif, are sufficient for DI activity. The N-terminus of TrbB_WT is disordered as indicated by a structural model of GST-TrbB_WT based on ColabFold-AlphaFold2 and Small Angle X-Ray Scattering data and ¹H–¹⁵N Heteronuclear Single Quantum Correlation (HSQC) spectroscopy of the untagged protein. This disordered region likely contributes to the protein's dynamicity; removal of this region results in a more stable protein based on ¹H–¹⁵N HSQC and Circular Dichroism Spectroscopies. Lastly, size exclusion chromatography analysis of TrbB_WT in the presence of TraW, a T4SS_F assembly protein predicted to interact with TrbB_WT, does not support the inference of a stable complex forming <em>in vitro</em>. This work advances our understanding of TrbB's structure and function, explores the role of structural disorder in protein dynamics in the context of a T4SS_F accessory protein, and highlights the importance of redox-assisted protein folding in the T4SS_F.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"8 ","pages":"Article 100156"},"PeriodicalIF":2.7,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X24000333/pdfft?md5=dd89ce99d737f5e271b30cb1909da8ae&pid=1-s2.0-S2665928X24000333-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141637070","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Natural flavonoid pectolinarin computationally targeted as a promising drug candidate against SARS-CoV-2","authors":"Mukta Rani ,&nbsp;Amit Kumar Sharma ,&nbsp;R.S. Chouhan ,&nbsp;Souvik Sur ,&nbsp;Rani Mansuri ,&nbsp;Rajesh K. Singh","doi":"10.1016/j.crstbi.2023.100120","DOIUrl":"https://doi.org/10.1016/j.crstbi.2023.100120","url":null,"abstract":"<div><p>Coronavirus disease-2019 (COVID-19) has become a global pandemic, necessitating the development of new medicines. In this investigation, we identified potential natural flavonoids and compared their inhibitory activity against spike glycoprotein, which is a target of SARS-CoV-2 and SARS-CoV. The target site for the interaction of new inhibitors for the treatment of SARS-CoV-2 has 82% sequence identity and the remaining 18% dissimilarities in RBD S1-subunit, S2-subunit, and 2.5% others. Molecular docking was employed to analyse the various binding processes used by each ligand in a library of 85 natural flavonoids that act as anti-viral medications and FDA authorised treatments for COVID-19. In the binding pocket of the target active site, remdesivir has less binding interaction than pectolinarin, according to the docking analysis. Pectolinarin is a natural flavonoid isolated from Cirsiumsetidensas that has anti-cancer, vasorelaxant, anti-inflammatory, hepatoprotective, anti-diabetic, anti-microbial, and anti-oxidant properties. The S-glycoprotein RBD region (330–583) is inhibited by kaempferol, rhoifolin, and herbacetin, but the S2 subunit (686–1270) is inhibited by pectolinarin, morin, and remdesivir. MD simulation analysis of S-glycoprotein of SARS-CoV-2 with pectolinarin complex at 100ns based on high dock-score. Finally, ADMET analysis was used to validate the proposed compounds with the highest binding energy.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100120"},"PeriodicalIF":2.8,"publicationDate":"2023-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X23000260/pdfft?md5=0876e4e16473c3913893c6e531b0f969&pid=1-s2.0-S2665928X23000260-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138839521","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Probing the ligand binding specificity of FNBP4 WW domains and interaction with FH1 domain of FMN1","authors":"Shubham Das,&nbsp;Sankar Maiti","doi":"10.1016/j.crstbi.2023.100119","DOIUrl":"https://doi.org/10.1016/j.crstbi.2023.100119","url":null,"abstract":"<div><p>Formins are a group of actin-binding proteins that mediate nascent actin filament polymerization, filament elongation, and barbed end-capping function, thereby regulating different cellular and developmental processes. Developmental processes like vertebrate gastrulation, neural growth cone dynamics, and limb development require formins functioning in a regulated manner. Formin-binding proteins like Rho GTPase regulate the activation of auto-inhibited conformation of diaphanous formins. Unlike other diaphanous formins, Formin1 (FMN1) a non-diaphanous formin is not regulated by Rho GTPase. FMN1 acts as an antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway during limb development. Several previous reports demonstrated that WW domain-containing proteins can interact with poly-proline-rich amino acid stretches of formins and play a crucial role in developmental processes. In contrast, WW domain-containing Formin-binding Protein 4 <strong>(</strong>FNBP4) protein plays an essential role in limb development. It has been hypothesized that the interaction between FNBP4 and FMN1 can further attribute to the role in limb development through the BMP signaling pathway. In this study, we have elucidated the binding kinetics of FNBP4 and FMN1 using surface plasmon resonance (SPR) and enzyme-linked immunosorbent assays (ELISA). Our findings confirm that the FNBP4 exhibits interaction with the poly-proline-rich formin homology 1 (FH1) domain of FMN1. Furthermore, only the first WW1 domains are involved in the interaction between the two domains. Thus, this study sheds light on the binding potentialities of WW domains of FNBP4 that might contribute to the regulation of FMN1 function.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100119"},"PeriodicalIF":2.8,"publicationDate":"2023-12-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X23000259/pdfft?md5=557180547c083e1b71ac124aa7c4ebf4&pid=1-s2.0-S2665928X23000259-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138656205","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Studying early structural changes in SOS1 mediated KRAS activation mechanism","authors":"Kirti Bhadhadhara,&nbsp;Vinod Jani,&nbsp;Shruti Koulgi,&nbsp;Uddhavesh Sonavane,&nbsp;Rajendra Joshi","doi":"10.1016/j.crstbi.2023.100115","DOIUrl":"10.1016/j.crstbi.2023.100115","url":null,"abstract":"<div><p>KRAS activation is known to be modulated by a guanine nucleotide exchange factor (GEF), namely, Son of Sevenless1 (SOS1). SOS1 facilitates the exchange of GDP to GTP thereby leading to activation of KRAS. The binding of GDP/GTP to KRAS at the REM/allosteric site of SOS1 regulates the activation of KRAS at CDC25/catalytic site by facilitating its exchange. Different aspects of the allosteric activation of KRAS through SOS1 are still being explored. To understand the SOS1 mediated activation of KRAS, molecular dynamics simulations for a total of nine SOS1 complexes (KRAS-SOS1-KRAS) were performed. These nine systems comprised different combinations of KRAS-bound nucleotides (GTP/GDP) at REM and CDC25 sites of SOS1. Various conformational and thermodynamic parameters were analyzed for these simulation systems. MMPBSA free energy analysis revealed that binding at CDC25 site of SOS1 was significantly low for GDP-bound KRAS as compared to that of GTP-bound KRAS. It was observed that presence of either GDP/GTP bound KRAS at the REM site of SOS1 affected the activation related changes in the KRAS present at CDC25 site. The conformational changes at the catalytic site of SOS1 resulting from GDP/GTP-bound KRAS at the allosteric changes may hint at KRAS activation through different pathways (slow/fast/rare). The allosteric effect on activation of KRAS at CDC25 site may be due to conformations adopted by switch-I, switch-II, beta2 regions of KRAS at REM site. The effect of structural rearrangements occurring at allosteric KRAS may have led to increased interactions between SOS1 and KRAS at both the sites. The SOS1 residues involved in these important interactions with KRAS at the REM site were R694, S732 and K735. Whereas the ones interacting with KRAS at CDC25 site were S807, W809 and K814. This may suggest the crucial role of these residues in guiding the allosteric activation of KRAS at CDC25 site. The conformational shifts observed in the switch-I, switch-II and alpha3 regions of KRAS at CDC25 site may be attributed to be a part of allosteric activation. The binding affinities, interacting residues and conformational dynamics may provide an insight into development of inhibitors targeting the SOS1 mediated KRAS activation.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100115"},"PeriodicalIF":2.8,"publicationDate":"2023-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X23000211/pdfft?md5=ba23f86d71877bd6e14dd387ed507c59&pid=1-s2.0-S2665928X23000211-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138624605","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural similarities between SAM and ATP recognition motifs and detection of ATP binding in a SAM binding DNA methyltransferase","authors":"Santhosh Sankar ,&nbsp;Preeti Preeti ,&nbsp;Kavya Ravikumar ,&nbsp;Amrendra Kumar ,&nbsp;Yedu Prasad ,&nbsp;Sukriti Pal ,&nbsp;Desirazu N. Rao ,&nbsp;Handanahal S. Savithri ,&nbsp;Nagasuma Chandra","doi":"10.1016/j.crstbi.2023.100108","DOIUrl":"https://doi.org/10.1016/j.crstbi.2023.100108","url":null,"abstract":"","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"6 ","pages":""},"PeriodicalIF":2.8,"publicationDate":"2023-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X23000144/pdfft?md5=58c2a7698f99ec6ba39e7a85575af79a&pid=1-s2.0-S2665928X23000144-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138436767","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cryo-EM structure of the trehalose monomycolate transporter, MmpL3, reconstituted into peptidiscs","authors":"Julie Couston ,&nbsp;Zongxin Guo ,&nbsp;Kaituo Wang ,&nbsp;Pontus Gourdon ,&nbsp;Mickaël Blaise","doi":"10.1016/j.crstbi.2023.100109","DOIUrl":"https://doi.org/10.1016/j.crstbi.2023.100109","url":null,"abstract":"<div><p>Mycobacteria have an atypical thick and waxy cell wall. One of the major building blocks of such mycomembrane is trehalose monomycolate (TMM). TMM is a mycolic acid ester of trehalose that possesses long acyl chains with up to 90 carbon atoms. TMM represents an essential component of mycobacteria and is synthesized in the cytoplasm, and then flipped over the plasma membrane by a specific transporter known as MmpL3. Over the last decade, MmpL3 has emerged as an attractive drug target to combat mycobacterial infections. Recent three-dimensional structures of MmpL3 determined by X-ray crystallography and cryo-EM have increased our understanding of the TMM transport, and the mode of action of inhibiting compounds. These structures were obtained in the presence of detergent and/or in a lipidic environment. In this study, we demonstrate the possibility of obtaining a high-quality cryo-EM structure of MmpL3 without any presence of detergent through the reconstitution of the protein into peptidiscs. The structure was determined at an overall resolution of 3.2 Å and demonstrates that the overall structure of MmpL3 is preserved as compared to previous structures. Further, the study identified a new structural arrangement of the linker that fuses the two subdomains of the transmembrane domain, suggesting the feature may serve a role in the transport process.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"6 ","pages":"Article 100109"},"PeriodicalIF":2.8,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X23000156/pdfft?md5=30d57577920410fae3129100020f9753&pid=1-s2.0-S2665928X23000156-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"134653072","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The conserved crown bridge loop at the catalytic centre of enzymes of the haloacid dehalogenase superfamily","authors":"David P. Leader,&nbsp;E. James Milner-White","doi":"10.1016/j.crstbi.2023.100105","DOIUrl":"10.1016/j.crstbi.2023.100105","url":null,"abstract":"<div><p>The crown bridge loop is hexapeptide motif in which the backbone carbonyl group at position 1 is hydrogen bonded to the backbone imino groups of positions 4 and 6. Residues at positions 1 and 4–6 are held in a tight substructure, but different orientations of the plane of the peptide bond between positions 2 and 3 result in two conformers: the 2,3-α_Rα_R crown bridge loop — found in approximately 7% of proteins — and the 2,3-β_Rα_L crown bridge loop, found in approximately 1–2% of proteins. We constructed a relational database in which we identified 60 instances of the 2,3-β_Rα_L conformer, and find that about half occur in enzymes of the haloacid dehalogenase (HAD) superfamily, where they are located next to the catalytic aspartate residue. Analysis of additional enzymes of the HAD superfamily in the extensive SCOPe dataset showed this crown bridge loop to be a conserved feature. Examination of available structures showed that the 2,3-β_Rα_L conformation — but not the 2,3-α_Rα_R conformation — allows the backbone carbonyl group at position 2 to interact with the essential Mg²⁺ ion. The possibility of interconversion between the 2,3-β_Rα_L and 2,3-α_Rα_R conformations during catalysis is discussed.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"6 ","pages":"Article 100105"},"PeriodicalIF":2.8,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/69/e8/main.PMC10541634.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41178270","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Soluble domains of cytochrome c-556 and Rieske iron–sulfur protein from Chlorobaculum tepidum: Crystal structures and interaction analysis","authors":"Hiraku Kishimoto ,&nbsp;Chihiro Azai ,&nbsp;Tomoya Yamamoto ,&nbsp;Risa Mutoh ,&nbsp;Tetsuko Nakaniwa ,&nbsp;Hideaki Tanaka ,&nbsp;Yohei Miyanoiri ,&nbsp;Genji Kurisu ,&nbsp;Hirozo Oh-oka","doi":"10.1016/j.crstbi.2023.100101","DOIUrl":"https://doi.org/10.1016/j.crstbi.2023.100101","url":null,"abstract":"<div><p>In photosynthetic green sulfur bacteria, the electron transfer reaction from menaquinol:cytochrome <em>c</em> oxidoreductase to the P840 reaction center (RC) complex occurs directly without any involvement of soluble electron carrier protein(s). X-ray crystallography has determined the three-dimensional structures of the soluble domains of the <em>CT0073</em> gene product and Rieske iron-sulfur protein (ISP). The former is a mono-heme cytochrome <em>c</em> with an α-absorption peak at 556 nm. The overall fold of the soluble domain of cytochrome <em>c</em>-556 (designated as cyt <em>c</em>-556_<em>sol</em>) consists of four α-helices and is very similar to that of water-soluble cyt <em>c</em>-554 that independently functions as an electron donor to the P840 RC complex. However, the latter's remarkably long and flexible loop between the α3 and α4 helices seems to make it impossible to be a substitute for the former. The structure of the soluble domain of the Rieske ISP (Rieske_<em>sol</em> protein) shows a typical β-sheets-dominated fold with a small cluster-binding and a large subdomain. The architecture of the Rieske_<em>sol</em> protein is bilobal and belongs to those of <em>b</em>₆<em>f</em>-type Rieske ISPs. Nuclear magnetic resonance (NMR) measurements revealed weak non-polar but specific interaction sites on Rieske_<em>sol</em> protein when mixed with cyt <em>c</em>-556_<em>sol</em>. Therefore, menaquinol:cytochrome <em>c</em> oxidoreductase in green sulfur bacteria features a Rieske/cyt<em>b</em> complex tightly associated with membrane-anchored cyt <em>c</em>-556.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"5 ","pages":"Article 100101"},"PeriodicalIF":2.8,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49813934","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Nature's soothing solution: Harnessing the potential of food-derived polysaccharides to control inflammation","authors":"Lucas de Freitas Pedrosa ,&nbsp;Paul de Vos ,&nbsp;João Paulo Fabi","doi":"10.1016/j.crstbi.2023.100112","DOIUrl":"https://doi.org/10.1016/j.crstbi.2023.100112","url":null,"abstract":"<div><p>Reducing inflammation by diet is a major goal for prevention or lowering symptoms of a variety of diseases, such as auto-immune reactions and cancers. Natural polysaccharides are increasingly gaining attention due to their potential immunomodulating capacity. Structures of those molecules are highly important for their effects on the innate immune system, cytokine production and secretion, and enzymes in immune cells. Such polysaccharides include β-glucans, pectins, fucoidans, and fructans. To better understand the potential of these immunomodulatory molecules, it is crucial to enhance dedicated research in the area. A bibliometric analysis was performed to set a starting observation point. Major pillars of inflammation, such as pattern recognition receptors (PRRs), enzymatic production of inflammatory molecules, and involvement in specific pathways such as Nuclear-factor kappa-B (NF-kB), involved in cell transcription, survival, and cytokine production, and mitogen-activated protein kinase (MAPK), a regulator of genetic expression, mitosis, and cell differentiation. Therefore, the outcomes from polysaccharide applications in those scenarios are discussed.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"6 ","pages":"Article 100112"},"PeriodicalIF":2.8,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X23000181/pdfft?md5=ec0180249c9abf086a14417e3c082f0c&pid=1-s2.0-S2665928X23000181-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"134653073","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Local heterogeneity analysis of crystallographic and cryo-EM maps using shell-approximation","authors":"Vladimir Y. Lunin ,&nbsp;Natalia L. Lunina ,&nbsp;Alexandre G. Urzhumtsev","doi":"10.1016/j.crstbi.2023.100102","DOIUrl":"10.1016/j.crstbi.2023.100102","url":null,"abstract":"<div><p>In X-ray crystallography and cryo-EM, experimental maps can be heterogeneous, showing different level of details in different regions. In this work we interpret heterogeneity in terms of two parameters, assigned individually for each atom, combining the conventional atomic displacement parameter with the resolution of the atomic image in the map. We propose a local real-space procedure to estimate the values of these heterogeneity parameters, assuming that a fragment of the density map and atomic positions are given. The procedure is based on an analytic representation of the atomic image, as a function of the inhomogeneity parameters and atomic coordinates. In this article, we report the results of the tests both with maps simulated and those derived from experimental data. For simulated maps containing regions with different resolutions, the method determines the local map resolution around the atomic centers and the values of the displacement parameter with reasonable accuracy. For experimental maps, obtained as a Fourier synthesis of a given global resolution, estimated values of the local resolution are close to the global one, and the values of the estimated displacement parameters are close to the respective values of the closest atoms in the refined model. Shown successful applications of the proposed method to experimental crystallographic and cryo-EM maps can be seen as a practical proof of method.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"6 ","pages":"Article 100102"},"PeriodicalIF":2.8,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/ff/50/main.PMC10329102.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9812483","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}