Journal of Structural Biology: X最新文献_第4页

Assessment of submicron bone tissue composition in plastic-embedded samples using optical photothermal infrared (O-PTIR) spectral imaging and machine learning 利用光学光热红外（O-PTIR）光谱成像和机器学习评估塑料包埋样本中的亚微米骨组织成分

IF 3.5

Journal of Structural Biology: X Pub Date : 2024-12-01 Epub Date: 2024-10-09 DOI: 10.1016/j.yjsbx.2024.100111

Isha Dev , Sofia Mehmood , Nancy Pleshko , Iyad Obeid , William Querido

{"title":"Assessment of submicron bone tissue composition in plastic-embedded samples using optical photothermal infrared (O-PTIR) spectral imaging and machine learning","authors":"Isha Dev , Sofia Mehmood , Nancy Pleshko , Iyad Obeid , William Querido","doi":"10.1016/j.yjsbx.2024.100111","DOIUrl":"10.1016/j.yjsbx.2024.100111","url":null,"abstract":"<div><div>Understanding the composition of bone tissue at the submicron level is crucial to elucidate factors contributing to bone disease and fragility. Here, we introduce a novel approach utilizing optical photothermal infrared (O-PTIR) spectroscopy and imaging coupled with machine learning analysis to assess bone tissue composition at 500 nm spatial resolution. This approach was used to evaluate thick bone samples embedded in typical poly(methyl methacrylate) (PMMA) blocks, eliminating the need for cumbersome thin sectioning. We demonstrate the utility of O-PTIR imaging to assess the distribution of bone tissue mineral and protein, as well as to explore the structure-composition relationship surrounding microporosity at a spatial resolution unattainable by conventional infrared imaging modalities. Using bone samples from wildtype (WT) mice and from a mouse model of osteogenesis imperfecta (OIM), we further showcase the application of O-PTIR spectroscopy to quantify mineral content, crystallinity, and carbonate content in spatially defined regions across the cortical bone. Notably, we show that machine learning analysis using support vector machine (SVM) was successful in identifying bone phenotypes (typical in WT, fragile in OIM) based on input of spectral data, with over 86 % of samples correctly identified when using the collagen spectral range. Our findings highlight the potential of O-PTIR spectroscopy and imaging as valuable tools for exploring bone submicron composition.</div></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"10 ","pages":"Article 100111"},"PeriodicalIF":3.5,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142530909","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}

引用次数: 0

Minimizing ice contamination during specimen preparation for cryo-soft X-ray tomography and cryo-electron tomography 尽量减少低温软 X 射线断层扫描和低温电子断层扫描标本制备过程中的冰污染

IF 3.5

Journal of Structural Biology: X Pub Date : 2024-12-01 Epub Date: 2024-10-18 DOI: 10.1016/j.yjsbx.2024.100113

Chia-Chun Hsieh, Zi-Jing Lin, Lee-Jene Lai

{"title":"Minimizing ice contamination during specimen preparation for cryo-soft X-ray tomography and cryo-electron tomography","authors":"Chia-Chun Hsieh, Zi-Jing Lin, Lee-Jene Lai","doi":"10.1016/j.yjsbx.2024.100113","DOIUrl":"10.1016/j.yjsbx.2024.100113","url":null,"abstract":"<div><div>Cryo-soft X-ray tomography (cryo-SXT) is a newly developed technique for imaging 3D whole cells in nearly native states. Cryo-SXT users require the preparation of numerous cryo-sample grids to use the allocated beamtime to study cellular phenomena under various conditions. Therefore, it is important to promptly prepare cryo-sample grids as efficiently and carefully as possible to minimize ice contamination on the frozen sample grid. In this study, we designed a cryo-multi-grid-box storage system, which includes a shell, funnel holder, and multi-grid-box container. Our system not only increases the number of cryo-sample grids that can be temporarily stored but also reduces the frequency of cryo grid-box container transfers, thus decreasing the probability of forming ice on the grid. We have also applied this system to A549 cryo cell grid preparation. The correlative images from cryo-light microscopy and cryo-SXT showed that limited ice had formed on the grid when preparation was performed using our system. Additionally, 3D images of mitochondria with the lamellar shape of the cristae could be observed in our cryo-SXT results. Our cryo-multi-grid-box storage system can be used for cryo-SXT and cryo-electron tomography (cryo-ET) applications.</div></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"10 ","pages":"Article 100113"},"PeriodicalIF":3.5,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142530489","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}

引用次数: 0

Localization of albumin with correlative super resolution light- and electron microscopy in the kidney 利用相关超分辨率光镜和电子显微镜确定肾脏中白蛋白的位置

IF 3.5

Journal of Structural Biology: X Pub Date : 2024-12-01 Epub Date: 2024-10-21 DOI: 10.1016/j.yjsbx.2024.100114

Alexandra N. Birtasu , Utz H. Ermel , Johanna V. Rahm , Anja Seybert , Benjamin Flottmann , Mike Heilemann , Florian Grahammer , Achilleas S. Frangakis

{"title":"Localization of albumin with correlative super resolution light- and electron microscopy in the kidney","authors":"Alexandra N. Birtasu , Utz H. Ermel , Johanna V. Rahm , Anja Seybert , Benjamin Flottmann , Mike Heilemann , Florian Grahammer , Achilleas S. Frangakis","doi":"10.1016/j.yjsbx.2024.100114","DOIUrl":"10.1016/j.yjsbx.2024.100114","url":null,"abstract":"<div><div>The functioning of vertebrate life relies on renal filtration of surplus fluid and elimination of low-molecular-weight waste products, while keeping serum proteins in the blood. In disease, however, there is leak of serum proteins and tracing them to identify the leaking position within tissue with a nanometer resolution poses a significant challenge. Correlative microscopy integrates the specificity of fluorescent protein labeling into high-resolution electron micrographs. Using chemical tagging of albumin with synthetic fluorophores we achieve protein-specific labeling that preserve their post-embedding fluorescence after high-pressure freezing and freeze-substitution of murine kidney tissue. Using advanced registration techniques for super-resolution correlative light and electron microscopy, we can localize the labeled albumin with a high precision in the x-y plane of electron micrographs and cartograph its distribution. Thereby we can quantify the albumin concentration and measure a linear reduction gradient across the kidney filtration barrier. Our study shows the feasibility of combining different microscopy contrasts for tracing fluorescently labeled protein markers with super resolution in various tissue samples and opens new perspectives for correlative imaging in volume electron microscopy.</div></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"10 ","pages":"Article 100114"},"PeriodicalIF":3.5,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142538214","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}

引用次数: 0

Editorial by Natalie Reznikov [for Buss et al., “Hierarchical organization of bone in three dimensions: A twist of twists” (2022)] Natalie Reznikov [为 Buss 等人撰写的社论《骨骼的三维分层组织：扭曲的扭曲"（2022 年］

IF 3.5

Journal of Structural Biology: X Pub Date : 2024-12-01 Epub Date: 2024-10-30 DOI: 10.1016/j.yjsbx.2024.100116

引用次数: 0

Do selectivity filter carbonyls in K+ channels flip away from the pore? Two-dimensional infrared spectroscopy study K+ 通道中的选择性过滤羰基是否会从孔中翻转？二维红外光谱研究

IF 3.5

Journal of Structural Biology: X Pub Date : 2024-12-01 Epub Date: 2024-07-15 DOI: 10.1016/j.yjsbx.2024.100108

Nikhil Maroli , Matthew J. Ryan , Martin T. Zanni , Alexei A. Kananenka

{"title":"Do selectivity filter carbonyls in K+ channels flip away from the pore? Two-dimensional infrared spectroscopy study","authors":"Nikhil Maroli , Matthew J. Ryan , Martin T. Zanni , Alexei A. Kananenka","doi":"10.1016/j.yjsbx.2024.100108","DOIUrl":"10.1016/j.yjsbx.2024.100108","url":null,"abstract":"<div><p>Molecular dynamics simulations revealed that the carbonyls of the Val residue in the conserved selectivity filter sequence TVGTG of potassium ion channels can flip away from the pore to form hydrogen bonds with the network of water molecules residing behind the selectivity filter. Such a configuration has been proposed to be relevant for C-type inactivation. Experimentally, X-ray crystallography of the KcsA channel admits the possibility that the Val carbonyls can flip, but it cannot decisively confirm the existence of such a configuration. In this study, we combined molecular dynamics simulations and line shape theory to design two-dimensional infrared spectroscopy experiments that can corroborate the existence of the selectivity filter configuration with flipped Val carbonyls. This ability to distinguish between flipped and unflipped carbonyls is based on the varying strength of the electric field inside and outside the pore, which is directly linked to carbonyl stretching frequencies that can be resolved using infrared spectroscopy.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"10 ","pages":"Article 100108"},"PeriodicalIF":3.5,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590152424000138/pdfft?md5=13bf2c257aaf33fbd68799a7ce5f4412&pid=1-s2.0-S2590152424000138-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141689647","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}

引用次数: 0

Structure of SARS-CoV-2 MTase nsp14 with the inhibitor STM957 reveals inhibition mechanism that is shared with a poxviral MTase VP39 SARS-CoV-2 MT 酶 nsp14 与抑制剂 STM957 的结构揭示了与痘病毒 MT 酶 VP39 共享的抑制机制

IF 3.5

Journal of Structural Biology: X Pub Date : 2024-12-01 Epub Date: 2024-07-29 DOI: 10.1016/j.yjsbx.2024.100109

Eva Zilecka, Martin Klima, Milan Stefek, Milan Dejmek, Radim Nencka, Evzen Boura

{"title":"Structure of SARS-CoV-2 MTase nsp14 with the inhibitor STM957 reveals inhibition mechanism that is shared with a poxviral MTase VP39","authors":"Eva Zilecka, Martin Klima, Milan Stefek, Milan Dejmek, Radim Nencka, Evzen Boura","doi":"10.1016/j.yjsbx.2024.100109","DOIUrl":"10.1016/j.yjsbx.2024.100109","url":null,"abstract":"<div><p>Nsp14 is an RNA methyltransferase (MTase) encoded by all coronaviruses. In fact, many viral families, including DNA viruses, encode MTases that catalyze the methylation of the RNA precap structure, resulting in fully capped viral RNA. This capping is crucial for efficient viral RNA translation, stability, and immune evasion. Our previous research identified nsp14 inhibitors based on the chemical scaffold of its methyl donor − the S-adenosyl methionine (SAM) − featuring a modified adenine base and a substituted arylsulfonamide. However, the binding mode of these inhibitors was based only on docking experiments. To uncover atomic details of nsp14 inhibition we solved the crystal structure of nsp14 bound to STM957. The structure revealed the atomic details of nsp14 inhibition such that the 7-deaza-adenine moiety of STM957 forms specific interactions with Tyr368, Ala353, and Phe367, while the arylsulfonamide moiety engages with Asn388 and Phe506. The large aromatic substituent at the 7-deaza position displaces a network of water molecules near the adenine base. Surprisingly, this was recently observed in the case of an unrelated monkeypox MTase VP39, where the 7-deaza modified SAH analogs also displaced water molecules from the vicinity of the active site.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"10 ","pages":"Article 100109"},"PeriodicalIF":3.5,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S259015242400014X/pdfft?md5=adc7af4fba68360ac9d28aa0d253354d&pid=1-s2.0-S259015242400014X-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141962088","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}

引用次数: 0

Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes 核酸结合 KH 结构域蛋白影响一系列生物通路，包括作为膜定位复合物的一部分发挥作用

IF 3.5

Journal of Structural Biology: X Pub Date : 2024-12-01 Epub Date: 2024-06-27 DOI: 10.1016/j.yjsbx.2024.100106

Md Kamrul Hasan , L. Jeannine Brady

{"title":"Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes","authors":"Md Kamrul Hasan , L. Jeannine Brady","doi":"10.1016/j.yjsbx.2024.100106","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2024.100106","url":null,"abstract":"<div><p>K-Homology domain (KH domain) proteins bind single-stranded nucleic acids, influence protein–protein interactions of proteins that harbor them, and are found in all kingdoms of life. In concert with other functional protein domains KH domains contribute to a variety of critical biological activities, often within higher order machineries including membrane-localized protein complexes. Eukaryotic KH domain proteins are linked to developmental processes, morphogenesis, and growth regulation, and their aberrant expression is often associated with cancer. Prokaryotic KH domain proteins are involved in integral cellular activities including cell division and protein translocation. Eukaryotic and prokaryotic KH domains share structural features, but are differentiated based on their structural organizations. In this review, we explore the structure/function relationships of known examples of KH domain proteins, and highlight cases in which they function within or at membrane surfaces. We also summarize examples of KH domain proteins that influence bacterial virulence and pathogenesis. We conclude the article by discussing prospective research avenues that could be pursued to better investigate this largely understudied protein category.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"10 ","pages":"Article 100106"},"PeriodicalIF":3.5,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590152424000114/pdfft?md5=0e422cb348e848d0c60e6c2df8352de4&pid=1-s2.0-S2590152424000114-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141486539","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}

引用次数: 0

Accurate size-based protein localization from cryo-ET tomograms 从低温电子断层扫描图中准确定位蛋白质大小

IF 3.5

Journal of Structural Biology: X Pub Date : 2024-12-01 Epub Date: 2024-06-26 DOI: 10.1016/j.yjsbx.2024.100104

Weisheng Jin , Ye Zhou , Alberto Bartesaghi

{"title":"Accurate size-based protein localization from cryo-ET tomograms","authors":"Weisheng Jin , Ye Zhou , Alberto Bartesaghi","doi":"10.1016/j.yjsbx.2024.100104","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2024.100104","url":null,"abstract":"<div><p>Cryo-electron tomography (cryo-ET) combined with sub-tomogram averaging (STA) allows the determination of protein structures imaged within the native context of the cell at near-atomic resolution. Particle picking is an essential step in the cryo-ET/STA image analysis pipeline that consists in locating the position of proteins within crowded cellular tomograms so that they can be aligned and averaged in 3D to improve resolution. While extensive work in 2D particle picking has been done in the context of single-particle cryo-EM, comparatively fewer strategies have been proposed to pick particles from 3D tomograms, in part due to the challenges associated with working with noisy 3D volumes affected by the missing wedge. While strategies based on 3D template-matching and deep learning are commonly used, these methods are computationally expensive and require either an external template or manual labelling which can bias the results and limit their applicability. Here, we propose a size-based method to pick particles from tomograms that is fast, accurate, and does not require external templates or user provided labels. We compare the performance of our approach against a commonly used algorithm based on deep learning, crYOLO, and show that our method: i) has higher detection accuracy, ii) does not require user input for labeling or time-consuming training, and iii) runs efficiently on non-specialized CPU hardware. We demonstrate the effectiveness of our approach by automatically detecting particles from tomograms representing different types of samples and using these particles to determine the high-resolution structures of ribosomes imaged <em>in vitro</em> and <em>in situ</em>.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"10 ","pages":"Article 100104"},"PeriodicalIF":3.5,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590152424000096/pdfft?md5=9bf56ad8420d48d82b350489a5b2005c&pid=1-s2.0-S2590152424000096-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141594447","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}

引用次数: 0

Conformational variability in the D2 loop of Plasmodium Apical Membrane antigen 1 疟原虫顶膜抗原 1 D2 环的构象变异性

IF 3.5

Journal of Structural Biology: X Pub Date : 2024-12-01 Epub Date: 2024-09-10 DOI: 10.1016/j.yjsbx.2024.100110

Frederick A. Saul , Brigitte Vulliez-Le Normand , Alexander Boes , Holger Spiegel , Clemens H.M. Kocken , Bart W. Faber , Graham A. Bentley

{"title":"Conformational variability in the D2 loop of Plasmodium Apical Membrane antigen 1","authors":"Frederick A. Saul , Brigitte Vulliez-Le Normand , Alexander Boes , Holger Spiegel , Clemens H.M. Kocken , Bart W. Faber , Graham A. Bentley","doi":"10.1016/j.yjsbx.2024.100110","DOIUrl":"10.1016/j.yjsbx.2024.100110","url":null,"abstract":"<div><p>Apical Membrane Antigen 1 (AMA1) plays a vital role in the invasion of the host erythrocyte by the malaria parasite, <em>Plasmodium</em>. It is thus an important target for vaccine and anti-malaria therapeutic strategies that block the invasion process. AMA1, present on the surface of the parasite, interacts with RON2, a component of the parasite’s rhoptry neck (RON) protein complex, which is transferred to the erythrocyte membrane during invasion. The D2 loop of AMA1 plays an essential role in invasion as it partially covers the RON2-binding site and must therefore be displaced for invasion to proceed. Several structural studies have shown that the D2 loop is very mobile, a property that is probably important for the function of AMA1. Here we present three crystal structures of AMA1 from <em>P. falciparum</em> (strains 3D7 and FVO) and <em>P. vivax</em> (strain Sal1), in which the D2 loop could be largely traced in the electron density maps. The D2 loop of PfAMA1-FVO and PvAMA1 (as a complex with a monoclonal antibody Fab) has a conformation previously noted in the <em>P. knowlesi</em> AMA1 structure. The D2 loop of PfAMA1-3D7, however, reveals a novel conformation. We analyse the conformational variability of the D2 loop in these structures, together with those previously reported. Three different conformations can be distinguished, all of which are highly helical and show some similarity in their secondary structure organisation. We discuss the significance of these observations in the light of the flexible nature of the D2 loop and its role in AMA1 function.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"10 ","pages":"Article 100110"},"PeriodicalIF":3.5,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590152424000151/pdfft?md5=18146cbe19a02e66f922067a1ea42cae&pid=1-s2.0-S2590152424000151-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142243547","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}

引用次数: 0

Grafting the ALFA tag for structural studies of aquaporin Z 接枝 ALFA 标签用于水蒸发蛋白 Z 的结构研究

IF 2.9

Journal of Structural Biology: X Pub Date : 2024-06-01 Epub Date: 2024-02-02 DOI: 10.1016/j.yjsbx.2024.100097

Lauren Stover , Hanieh Bahramimoghaddam , Lie Wang , Samantha Schrecke , Gaya P. Yadav , Ming Zhou , Arthur Laganowsky

{"title":"Grafting the ALFA tag for structural studies of aquaporin Z","authors":"Lauren Stover , Hanieh Bahramimoghaddam , Lie Wang , Samantha Schrecke , Gaya P. Yadav , Ming Zhou , Arthur Laganowsky","doi":"10.1016/j.yjsbx.2024.100097","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2024.100097","url":null,"abstract":"<div><p>Aquaporin Z (AqpZ), a bacterial water channel, forms a tetrameric complex and, like many other membrane proteins, activity is regulated by lipids. Various methods have been developed to facilitate structure determination of membrane proteins, such as the use of antibodies. Here, we graft onto AqpZ the ALFA tag (AqpZ-ALFA), an alpha helical epitope, to make use of the high-affinity anti-ALFA nanobody (nB). Native mass spectrometry reveals the AqpZ-ALFA fusion forms a stable, 1:1 complex with nB. Single-particle cryogenic electron microscopy studies reveal the octameric (AqpZ-ALFA)<sub>4</sub>(nB)<sub>4</sub> complex forms a dimeric assembly and the structure was determined to 1.9 Å resolution. Dimerization of the octamer is mediated through stacking of the symmetrically bound nBs. Tube-like density is also observed, revealing a potential cardiolipin binding site. Grafting of the ALFA tag, or other epitope, along with binding and association of nBs to promote larger complexes will have applications in structural studies and protein engineering.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"9 ","pages":"Article 100097"},"PeriodicalIF":2.9,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590152424000023/pdfft?md5=81782f0ee174ad218a60122e91b9a015&pid=1-s2.0-S2590152424000023-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139714608","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}

引用次数: 0