Journal of structural biology最新文献_第7页

Control of crystal growth during coccolith formation by the coccolithophore Gephyrocapsa oceanica 嗜茧动物 Gephyrocapsa oceanica 在茧石形成过程中对晶体生长的控制。

IF 3 3区生物学

Journal of structural biology Pub Date : 2024-02-11 DOI: 10.1016/j.jsb.2024.108066

Alexander Triccas , Fraser Laidlaw , Martin R. Singleton , Fabio Nudelman

{"title":"Control of crystal growth during coccolith formation by the coccolithophore Gephyrocapsa oceanica","authors":"Alexander Triccas , Fraser Laidlaw , Martin R. Singleton , Fabio Nudelman","doi":"10.1016/j.jsb.2024.108066","DOIUrl":"10.1016/j.jsb.2024.108066","url":null,"abstract":"<div><p>Coccolithophores are marine phytoplankton that produce calcite mineral scales called coccoliths. Many stages in the synthesis of these structures are still unresolved, making it difficult to accurately quantify the energetic costs involved in calcification, required to determine the response coccolith mineralization will have to rising ocean acidification and temperature created by an increase in global CO2 concentrations. To clarify this, an improved understanding of how coccolithophores control the fundamental processes of crystallization, including nucleation, growth, and morphology, is needed. Here, we study how crystal growth and morphology is controlled in the coccolithophore <em>Gephyrocapsa oceanica</em> by imaging coccoliths at various stages of maturity using cryo-transmission electron microscopy (cryoTEM), scanning electron microscopy (SEM) and focused ion beam SEM (FIB-SEM). We reveal that coccolith units tightly interlock with each other due to the non-vertical alignment of the two-layered tube element, causing these mineral units to extend over the adjacent crystals. In specific directions, the growth of the coccolith tube seems to be impacted by the physical constraint created by the close association of neighbouring units around the ring, influencing the overall morphology and organization of the crystals that develop. Our findings contribute to the overall understanding of how biological systems can manipulate crystallization to produce functional mineralized tissues.</p></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":null,"pages":null},"PeriodicalIF":3.0,"publicationDate":"2024-02-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1047847724000066/pdfft?md5=e650e944fc9dfcf785c724a2072652d9&pid=1-s2.0-S1047847724000066-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139729869","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Crystal structures of the fatty acid biosynthesis initiation enzymes in Bacillus subtilis 枯草芽孢杆菌脂肪酸生物合成启动酶的晶体结构

IF 3 3区生物学

Journal of structural biology Pub Date : 2024-02-03 DOI: 10.1016/j.jsb.2024.108065

Christopher D. Radka , Charles O. Rock

{"title":"Crystal structures of the fatty acid biosynthesis initiation enzymes in Bacillus subtilis","authors":"Christopher D. Radka , Charles O. Rock","doi":"10.1016/j.jsb.2024.108065","DOIUrl":"10.1016/j.jsb.2024.108065","url":null,"abstract":"<div><p>Bacteria use the fatty acid composition of membrane lipids to maintain homeostasis of the bilayer. β-Ketoacyl-ACP synthase III (FabH) initiates fatty acid biosynthesis and is the primary determinant of the fatty acid composition. FabH condenses malonyl-acyl carrier protein with an acyl-Coenzyme A primer to form β -ketoacyl-acyl carrier protein which is used to make substrates for lipid synthesis. The acyl-Coenzyme A primer determines whether an acyl chain in the membrane has iso, anteiso, or no branching (straight chain) and biophysical properties of the membrane. The soil bacterium <em>Bacillus subtilis</em> encodes two copies of FabH (<em>Bs</em>FabHA and <em>Bs</em>FabHB), and here we solve their crystal structures. The substrate-free 1.85 Å and 2.40 Å structures of <em>Bs</em>FabHA and <em>Bs</em>FabHB show both enzymes have similar residues that line the active site but differ in the architecture surrounding the catalytic residues and oxyanion hole. Branching in the <em>Bs</em>FabHB active site may better accommodate the structure of an iso-branched acyl-Coenzyme A molecule and thus confer superior utilization to <em>Bs</em>FabHA for this primer type. The 2.02 Å structure of <em>Bs</em>FabHA•Coenzyme A shows how the active site architecture changes after binding the first substrate. The other notable difference is an amino acid insertion in <em>Bs</em>FabHB that extends a cap that covers the dimer interface. The cap topology is diverse across FabH structures and appears to be a distinguishing feature. FabH enzymes have variable sensitivity to natural product inhibitors and the availability of crystal structures help clarify how nature designs antimicrobials that differentially target FabH homologs.</p></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":null,"pages":null},"PeriodicalIF":3.0,"publicationDate":"2024-02-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1047847724000054/pdfft?md5=241a6f10088e07721d7498722a671e26&pid=1-s2.0-S1047847724000054-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139678482","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Characterization of a new extra-axonemal structure in the Giardia intestinalis flagella 肠道贾第虫鞭毛中一种新的轴外结构的特征。

IF 3 3区生物学

Journal of structural biology Pub Date : 2024-01-26 DOI: 10.1016/j.jsb.2024.108064

Raphael Verdan , Beatriz Patricio , Gilberto Weismuller , Kildare Miranda , Wanderley de Souza , Marlene Benchimol , Ana Paula Gadelha

{"title":"Characterization of a new extra-axonemal structure in the Giardia intestinalis flagella","authors":"Raphael Verdan , Beatriz Patricio , Gilberto Weismuller , Kildare Miranda , Wanderley de Souza , Marlene Benchimol , Ana Paula Gadelha","doi":"10.1016/j.jsb.2024.108064","DOIUrl":"10.1016/j.jsb.2024.108064","url":null,"abstract":"<div><p>The inner structure of the flagella of <span><em>Giardia</em><em> intestinalis</em></span><span> is similar to that of other organisms, consisting of nine pairs of outer microtubules and a central pair containing radial spokes. Although the 9+2 axonemal structure is conserved, it is not clear whether subregions, including the transition zone, are present in the flagella of this parasite. </span><em>Giardia</em><span> axonemes<span> originate from basal bodies and have a lengthy cytosolic portion before becoming active flagella. The region of the emergence of the flagellum is not accompanied by any membrane specialization, as seen in other protozoa. Although </span></span><em>Giardia</em> is an intriguing model of study, few works focused on the ultrastructural analysis of the flagella of this parasite. Here, we analyzed the externalization region of the <em>G. intestinalis</em><span> flagella using ultra-high resolution scanning microscopy (with electrons and ions), atomic force microscopy<span> in liquid medium, freeze fracture, and electron tomography. Our data show that this region possesses a distinctive morphological feature – it extends outward and takes on a ring-like shape. When the plasma membrane is removed, a structure surrounding the axoneme becomes visible in this region. This new extra-axonemal structure is observed in all pairs of flagella of trophozoites and remains attached to the axoneme even when the interconnections between the axonemal microtubules are disrupted. High-resolution scanning electron microscopy provided insights into the arrangement of this structure, contributing to the characterization of the externalization region of the flagella of this parasite.</span></span></p></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":null,"pages":null},"PeriodicalIF":3.0,"publicationDate":"2024-01-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139570592","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A strained N-capping motif in α-helices of βαβ-units βαβ-单位的α-螺旋中的应变 N-封顶图案

IF 3 3区生物学

Journal of structural biology Pub Date : 2024-01-19 DOI: 10.1016/j.jsb.2024.108063

Anton M. Kargatov

引用次数: 0

Focused ion beam-SEM 3D study of osteodentin in the teeth of the Atlantic wolfish Anarhichas lupus 聚焦离子束-扫描电子显微镜对大西洋狼鱼牙齿中骨质素的三维研究

IF 3 3区生物学

Journal of structural biology Pub Date : 2024-01-13 DOI: 10.1016/j.jsb.2024.108062

Senthil Thangadurai , Marta Majkut , Joshua Milgram , Paul Zaslansky , Ron Shahar , Emeline Raguin

{"title":"Focused ion beam-SEM 3D study of osteodentin in the teeth of the Atlantic wolfish Anarhichas lupus","authors":"Senthil Thangadurai , Marta Majkut , Joshua Milgram , Paul Zaslansky , Ron Shahar , Emeline Raguin","doi":"10.1016/j.jsb.2024.108062","DOIUrl":"10.1016/j.jsb.2024.108062","url":null,"abstract":"<div><p>The palette of mineralized tissues in fish is wide, and this is particularly apparent in fish dentin. While the teeth of all vertebrates except fish contain a single dentinal tissue type, called orthodentin, dentin in the teeth of fish can be one of several different tissue types. The most common dentin type in fish is orthodentin. Orthodentin is characterized by several key structural features that are fundamentally different from those of bone and from those of osteodentin. Osteodentin, the second-most common dentin type in fish (based on the tiny fraction of fish species out of ∼30,000 extant fish species in which tooth structure was so far studied), is found in most Selachians (sharks and rays) as well as in several teleost species, and is structurally different from orthodentin.</p><p>Here we examine the hypothesis that osteodentin is similar to anosteocytic bone tissue in terms of its micro- and nano-structure. We use Focused Ion Beam-Scanning Electron Microscopy (FIB/SEM), as well as several other high-resolution imaging techniques, to characterize the 3D architecture of the three main components of osteodentin (denteons, inter-denteonal matrix, and the transition zone between them). We show that the matrix of osteodentin, although acellular, is extremely similar to mammalian osteonal bone matrix, both in general morphology and in the three-dimensional nano-arrangement of its mineralized collagen fibrils. We also document the presence of a complex network of nano-channels, similar to such networks recently described in bone. Finally, we document the presence of strings of hyper-mineralized small ‘pearls’ which surround the denteonal canals, and characterize their structure.</p></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":null,"pages":null},"PeriodicalIF":3.0,"publicationDate":"2024-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139463468","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structure of the prenyltransferase in bifunctional copalyl diphosphate synthase from Penicillium fellutanum reveals an open hexamer conformation 落羽青霉双功能共醛酰二磷酸合酶中的前酰基转移酶结构揭示了开放的六聚体构象

IF 3 3区生物学

Journal of structural biology Pub Date : 2024-01-05 DOI: 10.1016/j.jsb.2023.108060

Matthew N. Gaynes , Trey A. Ronnebaum , Kollin Schultz , Jacque L. Faylo , Ronen Marmorstein , David W. Christianson

{"title":"Structure of the prenyltransferase in bifunctional copalyl diphosphate synthase from Penicillium fellutanum reveals an open hexamer conformation","authors":"Matthew N. Gaynes , Trey A. Ronnebaum , Kollin Schultz , Jacque L. Faylo , Ronen Marmorstein , David W. Christianson","doi":"10.1016/j.jsb.2023.108060","DOIUrl":"10.1016/j.jsb.2023.108060","url":null,"abstract":"<div><p>Copalyl diphosphate synthase from <em>Penicillium fellutanum</em> (PfCPS) is an assembly-line terpene synthase that contains both prenyltransferase and class II cyclase activities. The prenyltransferase catalyzes processive chain elongation reactions using dimethylallyl diphosphate and three equivalents of isopentenyl diphosphate to yield geranylgeranyl diphosphate, which is then utilized as a substrate by the class II cyclase domain to generate copalyl diphosphate. Here, we report the 2.81 Å-resolution cryo-EM structure of the hexameric prenyltransferase of full-length PfCPS, which is surrounded by randomly splayed-out class II cyclase domains connected by disordered polypeptide linkers. The hexamer can be described as a trimer of dimers; surprisingly, one of the three dimer-dimer interfaces is separated to yield an open hexamer conformation, thus breaking the <em>D</em>3 symmetry typically observed in crystal structures of other prenyltransferase hexamers such as wild-type human GGPP synthase (hGGPPS). Interestingly, however, an open hexamer conformation was previously observed in the crystal structure of D188Y hGGPPS, apparently facilitated by hexamer-hexamer packing in the crystal lattice. The cryo-EM structure of the PfCPS prenyltransferase hexamer is the first to reveal that an open conformation can be achieved even in the absence of a point mutation or interaction with another hexamer. Even though PfCPS octamers are not detected, we suggest that the open hexamer conformation represents an intermediate in the hexamer-octamer equilibrium for those prenyltransferases that do exhibit oligomeric heterogeneity.</p></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":null,"pages":null},"PeriodicalIF":3.0,"publicationDate":"2024-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139105365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite 固态核磁共振 MAS CryoProbe 实现了与羟基磷灰石结合的人类血液蛋白玻璃连蛋白的结构研究

IF 3 3区生物学

Journal of structural biology Pub Date : 2024-01-05 DOI: 10.1016/j.jsb.2024.108061

T. Gopinath , Kyungsoo Shin , Ye Tian , Wonpil Im , Jochem Struppe , Barbara Perrone , Alia Hassan , Francesca M. Marassi

{"title":"Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite","authors":"T. Gopinath , Kyungsoo Shin , Ye Tian , Wonpil Im , Jochem Struppe , Barbara Perrone , Alia Hassan , Francesca M. Marassi","doi":"10.1016/j.jsb.2024.108061","DOIUrl":"10.1016/j.jsb.2024.108061","url":null,"abstract":"<div><p>The low sensitivity of nuclear magnetic resonance (NMR) is a major bottleneck for studying biomolecular structures of complex biomolecular assemblies. Cryogenically cooled probe technology overcomes the sensitivity limitations enabling NMR applications to challenging biomolecular systems. Here we describe solid-state NMR studies of the human blood protein vitronectin (Vn) bound to hydroxyapatite (HAP), the mineralized form of calcium phosphate, using a CryoProbe designed for magic angle spinning (MAS) experiments. Vn is a major blood protein that regulates many different physiological and pathological processes. The high sensitivity of the CryoProbe enabled us to acquire three-dimensional solid-state NMR spectra for sequential assignment and characterization of site-specific water-protein interactions that provide initial insights into the organization of the Vn-HAP complex. Vn associates with HAP in various pathological settings, including macular degeneration eyes and Alzheimer's disease brains. The ability to probe these assemblies at atomic detail paves the way for understanding their formation.</p></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":null,"pages":null},"PeriodicalIF":3.0,"publicationDate":"2024-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139105344","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Accurate, automatic determination of astigmatism and phase with Ctfplotter in IMOD 利用 IMOD 中的 Ctfplotter 准确、自动地确定散光和相位

IF 3 3区生物学

Journal of structural biology Pub Date : 2024-01-04 DOI: 10.1016/j.jsb.2023.108057

David N. Mastronarde

{"title":"Accurate, automatic determination of astigmatism and phase with Ctfplotter in IMOD","authors":"David N. Mastronarde","doi":"10.1016/j.jsb.2023.108057","DOIUrl":"10.1016/j.jsb.2023.108057","url":null,"abstract":"<div><p>Ctfplotter in the IMOD software package is a flexible program for determination of CTF parameters in tilt series images. It uses a novel approach to find astigmatism by measuring defocus in one-dimensional power spectra rotationally averaged over a series of restricted angular ranges. Comparisons with Ctffind, Gctf, and Warp show that Ctfplotter’s estimated astigmatism is generally more reliable than that found by these programs that fit CTF parameters to two-dimensional power spectra, especially at higher tilt angles. In addition to that intrinsic advantage, Ctfplotter can reduce the variability in astigmatism estimates further by summing results over multiple tilt angles (typically 5), while still finding defocus for each individual image. Its fitting strategy also produces better phase estimates. The program now includes features for tuning the sampling of the power spectrum so that it is well-represented for analysis, and for determining an appropriate fitting range that can vary with tilt angle. It can thus be used automatically in a variety of situations, not just for fitting tilt series, and has been integrated into the SerialEM acquisition software for real-time determination of focus and astigmatism.</p></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":null,"pages":null},"PeriodicalIF":3.0,"publicationDate":"2024-01-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139094457","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

DeepQs: Local quality assessment of cryo-EM density map by deep learning map-model fit score DeepQs：通过深度学习地图-模型拟合得分对低温电子显微镜密度图进行局部质量评估

IF 3 3区生物学

Journal of structural biology Pub Date : 2023-12-30 DOI: 10.1016/j.jsb.2023.108059

Ming-Feng Feng, Yu-Xuan Chen, Hong-Bin Shen

{"title":"DeepQs: Local quality assessment of cryo-EM density map by deep learning map-model fit score","authors":"Ming-Feng Feng, Yu-Xuan Chen, Hong-Bin Shen","doi":"10.1016/j.jsb.2023.108059","DOIUrl":"10.1016/j.jsb.2023.108059","url":null,"abstract":"<div><p>Cryogenic electron microscopy maps are valuable for determining macromolecule structures. A proper quality assessment method is essential for cryo-EM map selection or revision. This article presents DeepQs, a novel approach to estimate local quality for 3D cryo-EM density maps, using a deep-learning algorithm based on map-model fit score. DeepQs is a parameter-free method for users and incorporates structural information between map and its related atomic model into well-trained models by deep learning. More specifically, the DeepQs approach leverages the interplay between map and atomic model through predefined map-model fit score, Q-score. DeepQs can get close results to the ground truth map-model fit scores with only cryo-EM map as input. In experiments, DeepQs demonstrates the lowest root mean square error with standard method Fourier shell correlation metric and high correlation with map-model fit score, Q-score, when compared with other local quality estimation methods in high-resolution dataset (<=5 Å). DeepQs can also be applied to evaluate the quality of the post-processed maps. In both cases, DeepQs runs faster by using GPU acceleration. Our program is available at <span>http://www.csbio.sjtu.edu.cn/bioinf/DeepQs</span><svg><path></path></svg> for academic use.</p></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":null,"pages":null},"PeriodicalIF":3.0,"publicationDate":"2023-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139069956","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Cryo-forum: A framework for orientation recovery with uncertainty measure with the application in cryo-EM image analysis 低温论坛：在低温电子显微镜图像分析中应用带不确定性测量的定向恢复框架

IF 3 3区生物学

Journal of structural biology Pub Date : 2023-12-30 DOI: 10.1016/j.jsb.2023.108058

Szu-Chi Chung

{"title":"Cryo-forum: A framework for orientation recovery with uncertainty measure with the application in cryo-EM image analysis","authors":"Szu-Chi Chung","doi":"10.1016/j.jsb.2023.108058","DOIUrl":"10.1016/j.jsb.2023.108058","url":null,"abstract":"<div><p>In single-particle cryo-electron microscopy (cryo-EM), efficient determination of orientation parameters for particle images poses a significant challenge yet is crucial for reconstructing 3D structures. This task is complicated by the high noise levels in the datasets, which often include outliers, necessitating several time-consuming 2D clean-up processes. Recently, solutions based on deep learning have emerged, offering a more streamlined approach to the traditionally laborious task of orientation estimation. These solutions employ amortized inference, eliminating the need to estimate parameters individually for each image. However, these methods frequently overlook the presence of outliers and may not adequately concentrate on the components used within the network. This paper introduces a novel method using a 10-dimensional feature vector for orientation representation, extracting orientations as unit quaternions with an accompanying uncertainty metric. Furthermore, we propose a unique loss function that considers the pairwise distances between orientations, thereby enhancing the accuracy of our method. Finally, we also comprehensively evaluate the design choices in constructing the encoder network, a topic that has not received sufficient attention in the literature. Our numerical analysis demonstrates that our methodology effectively recovers orientations from 2D cryo-EM images in an end-to-end manner. Notably, the inclusion of uncertainty quantification allows for direct clean-up of the dataset at the 3D level. Lastly, we package our proposed methods into a user-friendly software suite named <em>cryo-forum</em>, designed for easy access by developers.</p></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":null,"pages":null},"PeriodicalIF":3.0,"publicationDate":"2023-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139069109","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0