Pub Date : 2025-11-01DOI: 10.1107/s2059798325008563
Frank Lennartz,Jan Wollenhaupt,Melanie Oelker,Paula Fröling,Uwe Mueller,Anke Deckers,Christoph Grathwol,Stefan Bräse,Nicole Jung,Manfred S Weiss
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to threaten global health. This underpins the need for novel therapeutics against this virus. Nonstructural protein 1 (Nsp1) of SARS-CoV-2 is a multifunctional protein with an essential role in viral replication. As such, it presents itself as an attractive target for drug discovery. Here, we describe two crystallographic fragment-screening campaigns against Nsp1, one using the established F2X-Entry Screen and one using a new, chemically and structurally diverse fragment library, which we call the KIT library. Together, 21 hits could be identified from 192 screened fragments, which constitutes the highest hit rate reported for Nsp1 to date. Many hits bind to a key functional region and interact with residues involved in cellular mRNA cleavage, ribosome binding and viral RNA recognition. Furthermore, most of the identified fragments share a common binding mode, providing promising starting points for further optimization into drug-like compounds that can disrupt the role of Nsp1 in viral replication.
{"title":"Crystallographic fragment screening against SARS-CoV-2 nonstructural protein 1 using the F2X-Entry Screen and a newly developed fragment library.","authors":"Frank Lennartz,Jan Wollenhaupt,Melanie Oelker,Paula Fröling,Uwe Mueller,Anke Deckers,Christoph Grathwol,Stefan Bräse,Nicole Jung,Manfred S Weiss","doi":"10.1107/s2059798325008563","DOIUrl":"https://doi.org/10.1107/s2059798325008563","url":null,"abstract":"Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to threaten global health. This underpins the need for novel therapeutics against this virus. Nonstructural protein 1 (Nsp1) of SARS-CoV-2 is a multifunctional protein with an essential role in viral replication. As such, it presents itself as an attractive target for drug discovery. Here, we describe two crystallographic fragment-screening campaigns against Nsp1, one using the established F2X-Entry Screen and one using a new, chemically and structurally diverse fragment library, which we call the KIT library. Together, 21 hits could be identified from 192 screened fragments, which constitutes the highest hit rate reported for Nsp1 to date. Many hits bind to a key functional region and interact with residues involved in cellular mRNA cleavage, ribosome binding and viral RNA recognition. Furthermore, most of the identified fragments share a common binding mode, providing promising starting points for further optimization into drug-like compounds that can disrupt the role of Nsp1 in viral replication.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"86 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145277392","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}
Pub Date : 2025-11-01DOI: 10.1107/s205979832500909x
Bao Di Ma,Xu Dong Kong
Methanol, a sustainable and cost-effective C1 compound, has been considered as a promising substrate for the biosynthesis of fuels and value-added chemicals. Synthetic methylotrophs have been developed by integrating natural methanol-assimilation pathways into non-native microbial hosts, with NAD+-dependent methanol dehydrogenases (MDHs) serving as attractive candidates for methanol oxidation. NAD+-dependent MDH1 from the methylotrophic bacterium Bacillus methanolicus MGA3 (BmMDH1) is one of the extensively studied MDHs. Although structural models of BmMDH1 had been proposed, its crystal structure had not been experimentally determined. In this study, the crystal structure of BmMDH1 is reported at 3.0 Å resolution. BmMDH1 forms a decamer made up of five dimers, stabilized by ionic and hydrogen-bonding interactions. Each monomer exhibits a conserved fold which is typical of the type III alcohol dehydrogenase family, comprising an N-terminal α/β dinucleotide-binding domain and a C-terminal all-α helical domain. Similar to other enzymes in this family, it has an NAD+-binding site formed by a Rossmann fold. As a metalloenzyme, BmMDH1 features a metal ion in its active site, coordinated by three histidine residues (His197, His262 and His276) and one aspartate residue (Asp193). Enzyme-activity assays identified Mn2+ as the most effective metal ion for supporting in vitro enzymatic activity. These findings provide essential structural insights for the rational engineering of methanol-utilizing biocatalysts, thereby advancing sustainable microbial biomanufacturing.
{"title":"Structural studies of NAD+-dependent methanol dehydrogenase 1 from Bacillus methanolicus MGA3.","authors":"Bao Di Ma,Xu Dong Kong","doi":"10.1107/s205979832500909x","DOIUrl":"https://doi.org/10.1107/s205979832500909x","url":null,"abstract":"Methanol, a sustainable and cost-effective C1 compound, has been considered as a promising substrate for the biosynthesis of fuels and value-added chemicals. Synthetic methylotrophs have been developed by integrating natural methanol-assimilation pathways into non-native microbial hosts, with NAD+-dependent methanol dehydrogenases (MDHs) serving as attractive candidates for methanol oxidation. NAD+-dependent MDH1 from the methylotrophic bacterium Bacillus methanolicus MGA3 (BmMDH1) is one of the extensively studied MDHs. Although structural models of BmMDH1 had been proposed, its crystal structure had not been experimentally determined. In this study, the crystal structure of BmMDH1 is reported at 3.0 Å resolution. BmMDH1 forms a decamer made up of five dimers, stabilized by ionic and hydrogen-bonding interactions. Each monomer exhibits a conserved fold which is typical of the type III alcohol dehydrogenase family, comprising an N-terminal α/β dinucleotide-binding domain and a C-terminal all-α helical domain. Similar to other enzymes in this family, it has an NAD+-binding site formed by a Rossmann fold. As a metalloenzyme, BmMDH1 features a metal ion in its active site, coordinated by three histidine residues (His197, His262 and His276) and one aspartate residue (Asp193). Enzyme-activity assays identified Mn2+ as the most effective metal ion for supporting in vitro enzymatic activity. These findings provide essential structural insights for the rational engineering of methanol-utilizing biocatalysts, thereby advancing sustainable microbial biomanufacturing.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"210 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145338721","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}
Pub Date : 2025-11-01DOI: 10.1107/s2059798325008332
Jonas Moecking,Tzviya Zeev-Ben-Mordehai
The explosion of cryo-electron microscopy (cryo-EM) over the last decade has brought with it a range of new approaches for gaining high-resolution structural information on previously inaccessible biological systems. Cryo-EM single-particle analysis (SPA) approaches typically entail overexpression and purification of the target protein. Larger and more complex molecular assemblies often require extensive optimization of the expression, purification and reconstitution procedures. Additionally, prior knowledge of the composition of the structure of interest is required. Approaches employing cryo-focused ion beam (FIB) milling and cryo-electron tomography (cryo-ET) have proven incredibly useful for exploring protein structures within cells while maintaining near-native conditions. Such strategies avoid purification of the target protein or protein complex, yet are often still limited in throughput and achievable resolution. Here, we highlight recent studies demonstrating that the range of samples suitable for SPA is expanding towards increasingly more native samples. We specifically focus on studies investigating complex macromolecular assemblies where tailored sample-preparation strategies made them amenable for SPA, while still keeping them in close-to-native conditions. These examples show that SPA has become a discovery tool for de novo protein identification and complex stoichiometry in more complex and thicker samples.
{"title":"Cryo-EM single-particle analysis expanding towards increasingly native samples.","authors":"Jonas Moecking,Tzviya Zeev-Ben-Mordehai","doi":"10.1107/s2059798325008332","DOIUrl":"https://doi.org/10.1107/s2059798325008332","url":null,"abstract":"The explosion of cryo-electron microscopy (cryo-EM) over the last decade has brought with it a range of new approaches for gaining high-resolution structural information on previously inaccessible biological systems. Cryo-EM single-particle analysis (SPA) approaches typically entail overexpression and purification of the target protein. Larger and more complex molecular assemblies often require extensive optimization of the expression, purification and reconstitution procedures. Additionally, prior knowledge of the composition of the structure of interest is required. Approaches employing cryo-focused ion beam (FIB) milling and cryo-electron tomography (cryo-ET) have proven incredibly useful for exploring protein structures within cells while maintaining near-native conditions. Such strategies avoid purification of the target protein or protein complex, yet are often still limited in throughput and achievable resolution. Here, we highlight recent studies demonstrating that the range of samples suitable for SPA is expanding towards increasingly more native samples. We specifically focus on studies investigating complex macromolecular assemblies where tailored sample-preparation strategies made them amenable for SPA, while still keeping them in close-to-native conditions. These examples show that SPA has become a discovery tool for de novo protein identification and complex stoichiometry in more complex and thicker samples.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"50 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145351659","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}
Pub Date : 2025-11-01DOI: 10.1107/s2059798325008356
Gayathri Yuvaraj,Kristoffer J M Lundgren,Elija Veenman,Esko Oksanen,Ulf Ryde
Particulate methane monooxygenase (pMMO) is an enzyme that converts methane into methanol at ambient temperature and pressure. Over the past three decades, the metal content and location of the active site have been highly controversial. Recent single-particle cryogenic electron-microscopy (cryo-EM) structures have furthered this debate. In this study, three cryo-EM structures (PDB entries 7s4h, 7s4j and 7ev9) are analysed by quantum refinement (QR). This approach augments traditional structural refinement with quantum-mechanical (QM) calculations for a small but interesting part of the protein (in this case, the copper sites). Our results indicate that the bis-His (CuA) site is correctly modelled as a mononuclear copper site in all three structures. The His-brace (CuB) site is also best modelled as mononuclear in all structures, although it was suggested to be a binuclear site in PDB entry 7ev9. The CuC site, which is observed only in PDB entry 7s4j, is correctly modelled and is probably reduced in the structure. The CuD putative active site, observed only in PDB entry 7s4h, is also mononuclear, but a water molecule might at least intermittently coordinate to the copper ion. On the other hand, our study does not find any support for the five additional copper ions suggested to be present in PDB entry 7ev9, including the suggested trinuclear active site and two sites in the so-called copper sponge. Instead, more chemically reasonable structures and better fit to both the cryo-EM and QM data are obtained if these copper ions are replaced with water molecules. This study illustrates the potential of QR as a standard component of cryo-EM studies for metal sites, for which reliable empirical restraints are missing.
{"title":"Critical evaluation of three cryo-EM structures of particulate methane monooxygenase by quantum refinement.","authors":"Gayathri Yuvaraj,Kristoffer J M Lundgren,Elija Veenman,Esko Oksanen,Ulf Ryde","doi":"10.1107/s2059798325008356","DOIUrl":"https://doi.org/10.1107/s2059798325008356","url":null,"abstract":"Particulate methane monooxygenase (pMMO) is an enzyme that converts methane into methanol at ambient temperature and pressure. Over the past three decades, the metal content and location of the active site have been highly controversial. Recent single-particle cryogenic electron-microscopy (cryo-EM) structures have furthered this debate. In this study, three cryo-EM structures (PDB entries 7s4h, 7s4j and 7ev9) are analysed by quantum refinement (QR). This approach augments traditional structural refinement with quantum-mechanical (QM) calculations for a small but interesting part of the protein (in this case, the copper sites). Our results indicate that the bis-His (CuA) site is correctly modelled as a mononuclear copper site in all three structures. The His-brace (CuB) site is also best modelled as mononuclear in all structures, although it was suggested to be a binuclear site in PDB entry 7ev9. The CuC site, which is observed only in PDB entry 7s4j, is correctly modelled and is probably reduced in the structure. The CuD putative active site, observed only in PDB entry 7s4h, is also mononuclear, but a water molecule might at least intermittently coordinate to the copper ion. On the other hand, our study does not find any support for the five additional copper ions suggested to be present in PDB entry 7ev9, including the suggested trinuclear active site and two sites in the so-called copper sponge. Instead, more chemically reasonable structures and better fit to both the cryo-EM and QM data are obtained if these copper ions are replaced with water molecules. This study illustrates the potential of QR as a standard component of cryo-EM studies for metal sites, for which reliable empirical restraints are missing.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"101 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145246776","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}
Pub Date : 2025-10-01DOI: 10.1107/s2059798325007831
O Lauzirika,M Pernica,D Herreros,E Ramírez-Aportela,J Krieger,M Gragera,M Iceta,P Conesa,Y Fonseca,J Jiménez,J Filipovic,J M Carazo,C O S Sorzano
Heterogeneity in cryoEM is essential for capturing the structural variability of macromolecules, reflecting their functional states and biological significance. However, estimating heterogeneity remains challenging due to particle misclassification and algorithmic biases, which can lead to reconstructions that blend distinct conformations or fail to resolve subtle differences. Furthermore, the low signal-to-noise ratio inherent in cryo-EM data makes it nearly impossible to detect minute structural changes, as noise often obscures subtle variations in macromolecular projections. In this paper, we investigate the use of p-values associated with the null hypothesis that the observed classification differs from a random partition of the input data set, thereby providing a statistical framework for determining the number of distinguishable classes present in a given data set.
{"title":"How many (distinguishable) classes can we identify in single-particle analysis?","authors":"O Lauzirika,M Pernica,D Herreros,E Ramírez-Aportela,J Krieger,M Gragera,M Iceta,P Conesa,Y Fonseca,J Jiménez,J Filipovic,J M Carazo,C O S Sorzano","doi":"10.1107/s2059798325007831","DOIUrl":"https://doi.org/10.1107/s2059798325007831","url":null,"abstract":"Heterogeneity in cryoEM is essential for capturing the structural variability of macromolecules, reflecting their functional states and biological significance. However, estimating heterogeneity remains challenging due to particle misclassification and algorithmic biases, which can lead to reconstructions that blend distinct conformations or fail to resolve subtle differences. Furthermore, the low signal-to-noise ratio inherent in cryo-EM data makes it nearly impossible to detect minute structural changes, as noise often obscures subtle variations in macromolecular projections. In this paper, we investigate the use of p-values associated with the null hypothesis that the observed classification differs from a random partition of the input data set, thereby providing a statistical framework for determining the number of distinguishable classes present in a given data set.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"37 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145018155","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}
Pub Date : 2025-10-01DOI: 10.1107/s2059798325007843
Christopher J Williams,Vincent B Chen,David C Richardson,Jane S Richardson
AlphaFold2 protein structure predictions are widely available for structural biology uses. These predictions, especially for eukaryotic proteins, frequently contain extensive regions predicted below the pLDDT = 70 level, the rule-of-thumb cutoff for high confidence. This work identifies major modes of behavior within low-pLDDT regions through a survey of human proteome predictions provided by the AlphaFold Protein Structure Database. The near-predictive mode resembles folded protein and can be a nearly accurate prediction. Barbed wire is extremely unprotein-like, being recognized by wide looping coils, an absence of packing contacts and numerous signature validation outliers, and it represents a region where the conformation has no predictive value. Pseudostructure presents an intermediate behavior with a misleading appearance of isolated and badly formed secondary-structure-like elements. These prediction modes are compared with annotations of disorder from MobiDB, showing general correlation between barbed wire/pseudostructure and many measures of disorder, an association between pseudostructure and signal peptides, and an association between near-predictive and regions of conditional folding. To enable users to identify these regions within a prediction, a new Phenix tool is developed encompassing the results of this work, including prediction annotation, visual markup and residue selection based on these prediction modes. This tool will help users develop expertise in interpreting difficult AlphaFold predictions and identify the near-predictive regions that can aid in molecular replacement when a prediction does not contain enough high-pLDDT regions.
{"title":"Categorizing prediction modes within low-pLDDT regions of AlphaFold2 structures: near-predictive, pseudostructure and barbed wire.","authors":"Christopher J Williams,Vincent B Chen,David C Richardson,Jane S Richardson","doi":"10.1107/s2059798325007843","DOIUrl":"https://doi.org/10.1107/s2059798325007843","url":null,"abstract":"AlphaFold2 protein structure predictions are widely available for structural biology uses. These predictions, especially for eukaryotic proteins, frequently contain extensive regions predicted below the pLDDT = 70 level, the rule-of-thumb cutoff for high confidence. This work identifies major modes of behavior within low-pLDDT regions through a survey of human proteome predictions provided by the AlphaFold Protein Structure Database. The near-predictive mode resembles folded protein and can be a nearly accurate prediction. Barbed wire is extremely unprotein-like, being recognized by wide looping coils, an absence of packing contacts and numerous signature validation outliers, and it represents a region where the conformation has no predictive value. Pseudostructure presents an intermediate behavior with a misleading appearance of isolated and badly formed secondary-structure-like elements. These prediction modes are compared with annotations of disorder from MobiDB, showing general correlation between barbed wire/pseudostructure and many measures of disorder, an association between pseudostructure and signal peptides, and an association between near-predictive and regions of conditional folding. To enable users to identify these regions within a prediction, a new Phenix tool is developed encompassing the results of this work, including prediction annotation, visual markup and residue selection based on these prediction modes. This tool will help users develop expertise in interpreting difficult AlphaFold predictions and identify the near-predictive regions that can aid in molecular replacement when a prediction does not contain enough high-pLDDT regions.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"41 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145035747","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}
Streptomyces griseolus CYP105A1 exhibits monooxygenase activity towards a wide variety of structurally diverse substrates with regiospecificity and stereospecificity, making it suitable for broad applications. Our previous studies have demonstrated that both wild-type CYP105A1 and its mutants metabolize vitamin D3 and its derivatives, as well as 12 types of nonsteroidal anti-inflammatory drugs (NSAIDs) and statins. Notably, the R84A mutant displayed high activity against vitamin D3, numerous NSAIDs and statins. Although we were unable to obtain CYP105A1-statin complex structures through co-crystallization and standard cryo data collection, we successfully acquired complex structures with mevastatin and simvastatin using room-temperature data collection with a conventional capillary method. We observed that the reduced unit-cell dimensions of the cryo crystals resulted in increased symmetry interactions, which induced cis-trans conversion of the peptide bond between Pro142 and Thr143 and conformational changes in the residues critical for statin binding. It is suggested that these increased symmetry interactions in the cryo crystals lead to dissociation of the statins from the active site of the enzyme.
{"title":"Room-temperature X-ray data collection enabled the structural determination of statin-bound CYP105A1.","authors":"Teisuke Takita,Sachiyo Yoneda,Kaori Yasuda,Kimihiko Mizutani,Kiyoshi Yasukawa,Toshiyuki Sakaki,Bunzo Mikami","doi":"10.1107/s2059798325007673","DOIUrl":"https://doi.org/10.1107/s2059798325007673","url":null,"abstract":"Streptomyces griseolus CYP105A1 exhibits monooxygenase activity towards a wide variety of structurally diverse substrates with regiospecificity and stereospecificity, making it suitable for broad applications. Our previous studies have demonstrated that both wild-type CYP105A1 and its mutants metabolize vitamin D3 and its derivatives, as well as 12 types of nonsteroidal anti-inflammatory drugs (NSAIDs) and statins. Notably, the R84A mutant displayed high activity against vitamin D3, numerous NSAIDs and statins. Although we were unable to obtain CYP105A1-statin complex structures through co-crystallization and standard cryo data collection, we successfully acquired complex structures with mevastatin and simvastatin using room-temperature data collection with a conventional capillary method. We observed that the reduced unit-cell dimensions of the cryo crystals resulted in increased symmetry interactions, which induced cis-trans conversion of the peptide bond between Pro142 and Thr143 and conformational changes in the residues critical for statin binding. It is suggested that these increased symmetry interactions in the cryo crystals lead to dissociation of the statins from the active site of the enzyme.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145078219","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}
Pub Date : 2025-10-01DOI: 10.1107/s2059798325007764
Marc Hebrant
Marc Hebrant provides a review of the second editon of Biophysical Chemistry by Dagmar Klostermeier and Markus G. Rudolph.
Marc Hebrant提供了Dagmar Klostermeier和Markus G. Rudolph的第二版生物物理化学的评论。
{"title":"Biophysical Chemistry, Second Edition. By Dagmar Klostermeier and Markus G. Rudolph. CRC Press, Boca Raton, 2025, pp. 944. ISBN 9781032060835. Price GBP 57.39 (hardback).","authors":"Marc Hebrant","doi":"10.1107/s2059798325007764","DOIUrl":"https://doi.org/10.1107/s2059798325007764","url":null,"abstract":"Marc Hebrant provides a review of the second editon of Biophysical Chemistry by Dagmar Klostermeier and Markus G. Rudolph.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"38 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144962805","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}
Pub Date : 2025-09-30DOI: 10.1107/s2059798325008599
Charles S Bond
Low-confidence regions in computational protein models have been identified to represent a largely untapped resource that may contain valuable structural information.
计算蛋白质模型中的低置信度区域已被确定为代表可能包含有价值的结构信息的大量未开发资源。
{"title":"Perspective on structure predictions of disorder.","authors":"Charles S Bond","doi":"10.1107/s2059798325008599","DOIUrl":"https://doi.org/10.1107/s2059798325008599","url":null,"abstract":"Low-confidence regions in computational protein models have been identified to represent a largely untapped resource that may contain valuable structural information.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"27 1","pages":"584"},"PeriodicalIF":0.0,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145194785","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}
Pub Date : 2025-09-01DOI: 10.1107/s205979832500628x
S Narasinga Rao,Manuel Soriano Garcia
Rengachary Parthasarathy is remembered.
人们记住了Rengachary Parthasarathy。
{"title":"Rengachary Parthasarathy (1939-2025): a life journey from Nagari to San Jose.","authors":"S Narasinga Rao,Manuel Soriano Garcia","doi":"10.1107/s205979832500628x","DOIUrl":"https://doi.org/10.1107/s205979832500628x","url":null,"abstract":"Rengachary Parthasarathy is remembered.","PeriodicalId":501686,"journal":{"name":"Acta Crystallographica Section D","volume":"16 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144791858","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}
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