IUCrJ最新文献

{"title":"Crystal structure of human peptidylarginine deiminase type VI (PAD6) provides insights into its inactivity","authors":"Fanomezana M. Ranaivoson ,&nbsp;Rieke Bande ,&nbsp;Isabell Cardaun ,&nbsp;Antonio De Riso ,&nbsp;Annette Gärtner ,&nbsp;Pui Loke ,&nbsp;Christina Reinisch ,&nbsp;Prasuna Vogirala ,&nbsp;Edward Beaumont ,&nbsp;J. L. Smith (Editor)","doi":"10.1107/S2052252524002549","DOIUrl":"10.1107/S2052252524002549","url":null,"abstract":"<div><p>The human peptidylarginine deiminase type VI (PAD6) is essential in oocyte and embryonic development as a component of the supramolecular assemblies called cytoplasmic lattices. The crystal structure presented here suggests PAD6 assembles as a dimer resembling other PADs, albeit with compromised abilities to bind Ca²⁺ and substrates. This aligns with existing <em>in vitro</em> data which indicate an enzymatically inactive isoform of PAD.</p></div><div><p>Human peptidylarginine deiminase isoform VI (PAD6), which is predominantly limited to cytoplasmic lattices in the mammalian oocytes in ovarian tissue, is essential for female fertility. It belongs to the peptidylarginine deiminase (PAD) enzyme family that catalyzes the conversion of arginine residues to citrulline in proteins. In contrast to other members of the family, recombinant PAD6 was previously found to be catalytically inactive. We sought to provide structural insight into the human homologue to shed light on this observation. We report here the first crystal structure of PAD6, determined at 1.7 Å resolution. PAD6 follows the same domain organization as other structurally known PAD isoenzymes. Further structural analysis and size-exclusion chromatography show that PAD6 behaves as a homodimer similar to PAD4. Differential scanning fluorimetry suggests that PAD6 does not coordinate Ca²⁺ which agrees with acidic residues found to coordinate Ca²⁺ in other PAD homologs not being conserved in PAD6. The crystal structure of PAD6 shows similarities with the inactive state of <em>apo</em> PAD2, in which the active site conformation is unsuitable for catalytic citrullination. The putative active site of PAD6 adopts a non-productive conformation that would not allow protein–substrate binding due to steric hindrance with rigid secondary structure elements. This observation is further supported by the lack of activity on the histone H3 and cytokeratin 5 substrates. These findings suggest a different mechanism for enzymatic activation compared with other PADs; alternatively, PAD6 may exert a non-enzymatic function in the cytoplasmic lattice of oocytes and early embryos.</p></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 3","pages":"Pages 395-404"},"PeriodicalIF":3.9,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140661838","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Chaperone-mediated MHC-I peptide exchange in antigen presentation","authors":"Jiansheng Jiang ,&nbsp;Kannan Natarajan ,&nbsp;David H. Margulies ,&nbsp;J. L. Smith (Editor)","doi":"10.1107/S2052252524002768","DOIUrl":"10.1107/S2052252524002768","url":null,"abstract":"<div><p>This topic review summarizes structures of chaperones complexed with MHC-I, the structural principles that govern peptide exchange and the mechanism in antigen presentation.</p></div><div><p>This work focuses on molecules that are encoded by the major histocompatibility complex (MHC) and that bind self-, foreign- or tumor-derived peptides and display these at the cell surface for recognition by receptors on T lymphocytes (T cell receptors, TCR) and natural killer (NK) cells. The past few decades have accumulated a vast knowledge base of the structures of MHC molecules and the complexes of MHC/TCR with specificity for many different peptides. In recent years, the structures of MHC-I molecules complexed with chaperones that assist in peptide loading have been revealed by X-ray crystallography and cryogenic electron microscopy. These structures have been further studied using mutagenesis, molecular dynamics and NMR approaches. This review summarizes the current structures and dynamic principles that govern peptide exchange as these relate to the process of antigen presentation.</p></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 3","pages":"Pages 287-298"},"PeriodicalIF":3.9,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140662862","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Time-series analysis of rhenium(I) organometallic covalent binding to a model protein for drug development","authors":"Francois J.F. Jacobs ,&nbsp;John R. Helliwell ,&nbsp;Alice Brink ,&nbsp;E. N. Baker (Editor)","doi":"10.1107/S2052252524002598","DOIUrl":"10.1107/S2052252524002598","url":null,"abstract":"<div><p>A detailed analysis of rhenium(I) organometallic covalent binding to a model protein is conducted at seven time points over 38 weeks. Changes in the protein structure induced at the Re binding sites over the time series as well as the relationship between the proximity of the solvent channels to the residues containing the highest-occupied Re are described.</p></div><div><p>Metal-based complexes with their unique chemical properties, including multiple oxidation states, radio-nuclear capabilities and various coordination geometries yield value as potential pharmaceuticals. Understanding the interactions between metals and biological systems will prove key for site-specific coordination of new metal-based lead compounds. This study merges the concepts of target coordination with fragment-based drug methodologies, supported by varying the anomalous scattering of rhenium along with infrared spectroscopy, and has identified rhenium metal sites bound covalently with two amino acid types within the model protein. A time-based series of lysozyme-rhenium-imidazole (HEWL-Re-Imi) crystals was analysed systematically over a span of 38 weeks. The main rhenium covalent coordination is observed at His15, Asp101 and Asp119. Weak (<em>i.e.</em> noncovalent) interactions are observed at other aspartic, asparagine, proline, tyrosine and tryptophan side chains. Detailed bond distance comparisons, including precision estimates, are reported, utilizing the diffraction precision index supplemented with small-molecule data from the Cambridge Structural Database. Key findings include changes in the protein structure induced at the rhenium metal binding site, not observed in similar metal-free structures. The binding sites are typically found along the solvent-channel-accessible protein surface. The three primary covalent metal binding sites are consistent throughout the time series, whereas binding to neighbouring amino acid residues changes through the time series. Co-crystallization was used, consistently yielding crystals four days after setup. After crystal formation, soaking of the compound into the crystal over 38 weeks is continued and explains these structural adjustments. It is the covalent bond stability at the three sites, their proximity to the solvent channel and the movement of residues to accommodate the metal that are important, and may prove useful for future radiopharmaceutical development including target modification.</p></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 3","pages":"Pages 359-373"},"PeriodicalIF":3.9,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140683057","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"3D electron diffraction goes multipolar","authors":"R. Beanland","doi":"10.1107/S2052252524003774","DOIUrl":"10.1107/S2052252524003774","url":null,"abstract":"<div><p>Over 30 years ago, it was shown that bonding between atoms has a noticeable effect on convergent beam electron diffraction patterns. The paper by Olech <em>et al.</em> [(2024). <em>IUCrJ</em>, <strong>11</strong>, 309–324] demonstrates that its influence is also clearly present in 3D electron diffraction data, opening up new possibilities for quantum crystallography.</p></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 3","pages":"Pages 277-278"},"PeriodicalIF":3.9,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11067748/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140851808","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A solid solution to computational challenges presented by crystal structures exhibiting disorder","authors":"Peter R. Spackman","doi":"10.1107/S2052252524001684","DOIUrl":"10.1107/S2052252524001684","url":null,"abstract":"<div><p>Crystal structues exhibiting disorder still present a barrier for many computational methods. Dittrich <em>et al.</em> [(2024). <em>IUCrJ</em>, <strong>11</strong>, 347–358] showcase a unified approach, tackling solid solutions, near symmetry and more.</p></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 3","pages":"Pages 275-276"},"PeriodicalIF":3.9,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11067745/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140860142","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cocrystals of a coumarin derivative: an efficient approach towards anti-leishmanial cocrystals against MIL-resistant Leishmania tropica","authors":"Muhammad Shahbaz ,&nbsp;Saba Farooq ,&nbsp;M. Iqbal Choudhary ,&nbsp;Sammer Yousuf ,&nbsp;L. R. MacGillivray (Editor)","doi":"10.1107/S2052252524001416","DOIUrl":"10.1107/S2052252524001416","url":null,"abstract":"&lt;div&gt;&lt;p&gt;This study demonstrates the synthesis of non-cytotoxic active candidates (co-crystals) of coumarin-3-carb­oxy­lic acid with various coformers to target the MIL-resistant &lt;em&gt;Leishmania tropica&lt;/em&gt;. These promising anti-leishmanial results indicate the importance of crystal engineering by highlighting that manipulation of supramolecular architecture in the solid state can impact the biological response.&lt;/p&gt;&lt;/div&gt;&lt;div&gt;&lt;p&gt;Leishmaniasis is a neglected parasitic tropical disease with numerous clinical manifestations. One of the causative agents of cutaneous leishmaniasis (CL) is &lt;em&gt;Leishmania tropica&lt;/em&gt; (&lt;em&gt;L. tropica&lt;/em&gt;) known for causing ulcerative lesions on the skin. The adverse effects of the recommended available drugs, such as amphotericin B and pentavalent antimonial, and the emergence of drug resistance in parasites, mean the search for new safe and effective anti-leishmanial agents is crucial. Miltefosine (MIL) was the first recommended oral medication, but its use is now limited because of the rapid emergence of resistance. Pharmaceutical cocrystallization is an effective method to improve the physicochemical and biological properties of active pharmaceutical ingredients (APIs). Herein, we describe the cocrystallization of coumarin-3-carb­oxy­lic acid (&lt;strong&gt;CU&lt;/strong&gt;, &lt;strong&gt;1a&lt;/strong&gt;; 2-oxobenzo­pyrane-3-carb­oxy­lic acid, C&lt;sub&gt;10&lt;/sub&gt;H&lt;sub&gt;6&lt;/sub&gt;O&lt;sub&gt;4&lt;/sub&gt;) with five coformers [2-amino-3-bromo­pyridine (&lt;strong&gt;1b&lt;/strong&gt;), 2-amino-5-(tri­fluoro­methyl)-pyridine (&lt;strong&gt;1c&lt;/strong&gt;), 2-amino-6-methyl­pyridine (&lt;strong&gt;1d&lt;/strong&gt;), &lt;em&gt;p&lt;/em&gt;-amino­benzoic acid (&lt;strong&gt;1e&lt;/strong&gt;) and amitrole (&lt;strong&gt;1f&lt;/strong&gt;)] in a 1:1 stoichiometric ratio via the neat grinding method. The cocrystals &lt;strong&gt;2&lt;/strong&gt;–&lt;strong&gt;6&lt;/strong&gt; obtained were characterized via single-crystal X-ray diffraction, powder X-ray diffraction, differential scanning calorimetry and thermogravimetric analysis, as well as Fourier transform infrared spectroscopy. Non-covalent interactions, such as van der Waals, hydrogen bonding, C—H⋯π and π⋯π interactions contribute significantly towards the packing of a crystal structure and alter the physicochemical and biological activity of &lt;strong&gt;CU&lt;/strong&gt;. In this research, newly synthesized cocrystals were evaluated for their anti-leishmanial activity against the MIL-resistant &lt;em&gt;L. tropica&lt;/em&gt; and cytotoxicity against the 3T3 (normal fibroblast) cell line. Among the non-cytotoxic cocrystals synthesized (&lt;strong&gt;2&lt;/strong&gt;–&lt;strong&gt;6&lt;/strong&gt;), &lt;strong&gt;CU&lt;/strong&gt;:&lt;strong&gt;1b&lt;/strong&gt; (&lt;strong&gt;2&lt;/strong&gt;, IC&lt;sub&gt;50&lt;/sub&gt; = 61.83 ± 0.59 µ&lt;em&gt;M&lt;/em&gt;), &lt;strong&gt;CU&lt;/strong&gt;:&lt;strong&gt;1c&lt;/strong&gt; (&lt;strong&gt;3&lt;/strong&gt;, 125.7 ± 1.15 µ&lt;em&gt;M&lt;/em&gt;) and &lt;strong&gt;CU&lt;/strong&gt;:&lt;strong&gt;1d&lt;/strong&gt; (&lt;strong&gt;4&lt;/strong&gt;, 48.71 ± 0.75 µ&lt;em&gt;M&lt;/em&gt;) appeared to be potent anti-leishmanial agents and showed several-fold more anti-leishmanial potential than the tested standard drug (MIL, IC&lt;sub&gt;50&lt;/sub&gt; = 169.55 ± 0.078 ","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 2","pages":"Pages 224-236"},"PeriodicalIF":3.9,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10916291/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140012588","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural analysis of nanocrystals by pair distribution function combining electron diffraction with crystal tilting","authors":"Linshuo Guo ,&nbsp;Shitao Wu ,&nbsp;Zhengyang Zhou ,&nbsp;Yanhang Ma ,&nbsp;M. Gemmi (Editor)","doi":"10.1107/S2052252524001064","DOIUrl":"10.1107/S2052252524001064","url":null,"abstract":"<div><p>A new method is proposed to enhance the continuity of diffraction rings and improve the signal-to-noise ratio in electron diffraction data for electron pair distribution function (ePDF) analysis.</p></div><div><p>As an important characterization method, pair distribution function (PDF) has been extensively used in structural analysis of nanomaterials, providing key insights into the degree of crystallinity, atomic structure, local disorder <em>etc</em>. The collection of scattering signals with good statistics is necessary for a reliable structural analysis. However, current conventional electron diffraction experiments using PDF (ePDF) are limited in their ability to acquire continuous diffraction rings for large nanoparticles. Herein, a new method – tilt-ePDF – is proposed to improve the data quality and compatibility of ePDF by a combination of electron diffraction and specimen tilting. In the present work, a tilt-series of electron diffraction patterns was collected from gold nanoparticles with three different sizes and a standard sample polycrystalline aluminium film for ePDF analysis. The results show that tilt-ePDF can not only enhance the continuity of diffraction rings, but can also improve the signal-to-noise ratio in the high scattering angle range. As a result, compared with conventional ePDF data, tilt-ePDF data provide structure parameters with a better accuracy and lower residual factors in the refinement against the crystal structure. This method provides a new way of utilizing ePDF to obtain accurate local structure information from nanoparticles.</p></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 2","pages":"Pages 202-209"},"PeriodicalIF":3.9,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10916296/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139741078","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterizing self-assembled structures made with magnetic Janus nanoparticles","authors":"Elizabeth Blackburn","doi":"10.1107/S2052252524001532","DOIUrl":"10.1107/S2052252524001532","url":null,"abstract":"<div><p>Small-angle X-ray scattering has revealed how magnetic Janus particles pair up in solutions in small and large magnetic fields.</p></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 2","pages":"Pages 131-132"},"PeriodicalIF":3.9,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10916292/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140012587","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Community recommendations on cryoEM data archiving and validation","authors":"Gerard J. Kleywegt ,&nbsp;Paul D. Adams ,&nbsp;Sarah J. Butcher ,&nbsp;Catherine L. Lawson ,&nbsp;Alexis Rohou ,&nbsp;Peter B. Rosenthal ,&nbsp;Sriram Subramaniam ,&nbsp;Maya Topf ,&nbsp;Sanja Abbott ,&nbsp;Philip R. Baldwin ,&nbsp;John M. Berrisford ,&nbsp;Gérard Bricogne ,&nbsp;Preeti Choudhary ,&nbsp;Tristan I. Croll ,&nbsp;Radostin Danev ,&nbsp;Sai J. Ganesan ,&nbsp;Timothy Grant ,&nbsp;Aleksandras Gutmanas ,&nbsp;Richard Henderson ,&nbsp;J. Bernard Heymann ,&nbsp;S. Raunser (Editor)","doi":"10.1107/S2052252524001246","DOIUrl":"10.1107/S2052252524001246","url":null,"abstract":"<div><p>This white paper describes recommendations to the wwPDB, EMDB and the cryoEM communities regarding archiving and validation of single-particle structures and volumes.</p></div><div><p>In January 2020, a workshop was held at EMBL-EBI (Hinxton, UK) to discuss data requirements for the deposition and validation of cryoEM structures, with a focus on single-particle analysis. The meeting was attended by 47 experts in data processing, model building and refinement, validation, and archiving of such structures. This report describes the workshop’s motivation and history, the topics discussed, and the resulting consensus recommendations. Some challenges for future methods-development efforts in this area are also highlighted, as is the implementation to date of some of the recommendations.</p></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 2","pages":"Pages 140-151"},"PeriodicalIF":3.9,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10916293/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139735235","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Solving protein structures by combining structure prediction, molecular replacement and direct-methods-aided model completion","authors":"Zengru Li ,&nbsp;Haifu Fan ,&nbsp;Wei Ding ,&nbsp;Z.-J. Liu (Editor)","doi":"10.1107/S2052252523010291","DOIUrl":"10.1107/S2052252523010291","url":null,"abstract":"<div><p>We propose a direct-methods-based dual-space iteration strategy for model completion of molecular replacement (MR) with predicted models. Direct methods has been demonstrated as a powerful tool for phase optimization in protein crystallography, whereas the dual-space iterative strategy is particularly suitable for solving crystallographic protein-complex structures starting from a small subunit. This combined approach provides a shortcut in simplifying the pre-processing steps of predicted models for MR and for final model completion.</p></div><div><p>Highly accurate protein structure prediction can generate accurate models of protein and protein–protein complexes in X-ray crystallography. However, the question of how to make more effective use of predicted models for completing structure analysis, and which strategies should be employed for the more challenging cases such as multi-helical structures, multimeric structures and extremely large structures, both in the model preparation and in the completion steps, remains open for discussion. In this paper, a new strategy is proposed based on the framework of direct methods and dual-space iteration, which can greatly simplify the pre-processing steps of predicted models both in normal and in challenging cases. Following this strategy, full-length models or the conservative structural domains could be used directly as the starting model, and the phase error and the model bias between the starting model and the real structure would be modified in the direct-methods-based dual-space iteration. Many challenging cases (from CASP14) have been tested for the general applicability of this constructive strategy, and almost complete models have been generated with reasonable statistics. The hybrid strategy therefore provides a meaningful scheme for X-ray structure determination using a predicted model as the starting point.</p></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 2","pages":"Pages 152-167"},"PeriodicalIF":3.9,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10916285/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139424780","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}