Pub Date : 2023-07-07DOI: 10.1107/s2053273323098881
Peter W. Stephens, Rasika H. V. Dias, Andrey A. Yakovenko
Purification of ethylene from ethylene -ethane mixtures is an important and challenging industrial process, currently performed by highly energy-intensive cryogenic distillation. We have been studying the reversible reaction of C2H4 with various molecular pyrazolate complexes of copper, and fi nd that they are extremely selective for ethylene vs. ethane.1 -4 A typical gas-phase adsorption/desorption reaction, which occurs at 320 K – 343 K at atmospheric pressure, is illustrated in Fig. 1. We have performed in situ powder diffraction measurements of the repeated adsorption and desorption of ethylene from dense powders of several copper pyrazolate complexes at beamline 17 - BM of the Advanced Photon Source.2,3 We have determined previously unknown structures of several of the compounds and monitor the conversion between phases with and without adsorbed ethylene. It is truly remarkable that the subject molecules reversibly pass between trimer and dimer structures in the solid state upon reaction with ethylene.
{"title":"In situ studies of molecular copper compounds for highly selective purification of ethylene","authors":"Peter W. Stephens, Rasika H. V. Dias, Andrey A. Yakovenko","doi":"10.1107/s2053273323098881","DOIUrl":"https://doi.org/10.1107/s2053273323098881","url":null,"abstract":"Purification of ethylene from ethylene -ethane mixtures is an important and challenging industrial process, currently performed by highly energy-intensive cryogenic distillation. We have been studying the reversible reaction of C2H4 with various molecular pyrazolate complexes of copper, and fi nd that they are extremely selective for ethylene vs. ethane.1 -4 A typical gas-phase adsorption/desorption reaction, which occurs at 320 K – 343 K at atmospheric pressure, is illustrated in Fig. 1. We have performed in situ powder diffraction measurements of the repeated adsorption and desorption of ethylene from dense powders of several copper pyrazolate complexes at beamline 17 - BM of the Advanced Photon Source.2,3 We have determined previously unknown structures of several of the compounds and monitor the conversion between phases with and without adsorbed ethylene. It is truly remarkable that the subject molecules reversibly pass between trimer and dimer structures in the solid state upon reaction with ethylene.","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"22 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139362151","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 : 2023-07-07DOI: 10.1107/s2053273323096304
Christopher J. Williams, Sushrit Pasumarthy, Jane S Richardson
Disulfide bridges between cysteine sidechains are one of the more unusual features of protein macromolecules. They provide a strong, stabilizing, covalent connection between sequence - distant parts of a protein. Previous efforts by the Richardson Lab to compile a comprehensive library of disulfide conformations were frustrated by our datasets being in sufficiently large in the face of the huge conformational space afforded by disulfides’ 5 chi torsions (more than lysine!). Now, enabled by the Top2018 dataset, we present our survey of disulfide bridges. Disulfides have great conformational diversity. This diversity is matched by the diversity of proteins and structural contexts they appear in. Nevertheless, disulfide conformations are often conserved among proteins with similar functions. Some conformations are even unique to certain protein families. Others are conserved according to their position relative to secondary structure. This library will aid in selection of appropriate disulfides in model building and in MolProbity-style validation of experimental and predicted models.
{"title":"A disulfide bridge survey and library","authors":"Christopher J. Williams, Sushrit Pasumarthy, Jane S Richardson","doi":"10.1107/s2053273323096304","DOIUrl":"https://doi.org/10.1107/s2053273323096304","url":null,"abstract":"Disulfide bridges between cysteine sidechains are one of the more unusual features of protein macromolecules. They provide a strong, stabilizing, covalent connection between sequence - distant parts of a protein. Previous efforts by the Richardson Lab to compile a comprehensive library of disulfide conformations were frustrated by our datasets being in sufficiently large in the face of the huge conformational space afforded by disulfides’ 5 chi torsions (more than lysine!). Now, enabled by the Top2018 dataset, we present our survey of disulfide bridges. Disulfides have great conformational diversity. This diversity is matched by the diversity of proteins and structural contexts they appear in. Nevertheless, disulfide conformations are often conserved among proteins with similar functions. Some conformations are even unique to certain protein families. Others are conserved according to their position relative to secondary structure. This library will aid in selection of appropriate disulfides in model building and in MolProbity-style validation of experimental and predicted models.","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139362156","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 : 2023-07-07DOI: 10.1107/s205327332309928x
Gabrielle R. Budziszewski, Tiffany R. Wright, M. E. Snell, Miranda L. Lynch, Sarah E J Bowman
{"title":"Operations of the National Crystallization Center: two decades of high-throughput crystallization efforts fueled by structural genomics","authors":"Gabrielle R. Budziszewski, Tiffany R. Wright, M. E. Snell, Miranda L. Lynch, Sarah E J Bowman","doi":"10.1107/s205327332309928x","DOIUrl":"https://doi.org/10.1107/s205327332309928x","url":null,"abstract":"","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"3 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139362173","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 : 2023-07-07DOI: 10.1107/s2053273323097619
Nick Vukotic, Anton Dmitrienko
{"title":"Innovating together: how strategic academic–industry collaboration can drive advances in materials discovery and create economic and socio-economic benefits","authors":"Nick Vukotic, Anton Dmitrienko","doi":"10.1107/s2053273323097619","DOIUrl":"https://doi.org/10.1107/s2053273323097619","url":null,"abstract":"","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"20 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139361665","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 : 2023-07-07DOI: 10.1107/s2053273323097097
Shuchismita Dutta
{"title":"Developing training and educational resources in biomolecular structural biology for diverse audiences","authors":"Shuchismita Dutta","doi":"10.1107/s2053273323097097","DOIUrl":"https://doi.org/10.1107/s2053273323097097","url":null,"abstract":"","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"26 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139361681","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 : 2023-07-07DOI: 10.1107/s2053273323097346
Jonathan R. Herrmann, Natalie Young, A. Kotecha
X - ray diffraction using synchrotron radiation established a routine single-crystal structure determination workflow for small and macromolecules; however, these experiments require large, well -ordered crystals (50 - 100 μm). Growing large protein crystals is a critical bottleneck that is either time-consuming or challenging to overcome, and often smaller crystals are more attainable. Although microfocus beamlines can analyze crystals as small as 10 - 50 μm, they are prone to radiation damage or diffract X - rays weakly, limiting achievable resolution. Electrons are more advantageous than X - rays for the analysis of very small crystals (well below 1 μm in size) because accelerated electrons scatter more readily than X - rays, resulting in a stronger signal from thinner samples. Micro - or nano-crystal elect ron diffraction (MicroED) is thus well - suited for the analysis of small crystals, producing high-resolution 3D structures of small chemical compounds or biological macromolecules. MicroED
利用同步辐射进行 X 射线衍射为小分子和大分子结构测定建立了常规的单晶结构测定工作流程；然而，这些实验需要大而有序的晶体（50 - 100 μm）。生长大型蛋白质晶体是一个关键的瓶颈，要么耗时，要么难以克服，通常较小的晶体更容易实现。虽然微聚焦光束线可以分析小至 10 - 50 微米的晶体，但它们容易受到辐射损伤，或对 X 射线的折射较弱，从而限制了可达到的分辨率。在分析极小晶体（尺寸远小于 1 微米）时，电子比 X 射线更有优势，因为加速电子比 X 射线更容易散射，从而从更薄的样品中获得更强的信号。因此，微米或纳米晶体电子衍射（MicroED）非常适合分析小晶体，生成小化合物或生物大分子的高分辨率三维结构。微电子衍射
{"title":"A complete micro-electron diffraction (MicroED) solution for fast structure determination of macromolecules and small molecules","authors":"Jonathan R. Herrmann, Natalie Young, A. Kotecha","doi":"10.1107/s2053273323097346","DOIUrl":"https://doi.org/10.1107/s2053273323097346","url":null,"abstract":"X - ray diffraction using synchrotron radiation established a routine single-crystal structure determination workflow for small and macromolecules; however, these experiments require large, well -ordered crystals (50 - 100 μm). Growing large protein crystals is a critical bottleneck that is either time-consuming or challenging to overcome, and often smaller crystals are more attainable. Although microfocus beamlines can analyze crystals as small as 10 - 50 μm, they are prone to radiation damage or diffract X - rays weakly, limiting achievable resolution. Electrons are more advantageous than X - rays for the analysis of very small crystals (well below 1 μm in size) because accelerated electrons scatter more readily than X - rays, resulting in a stronger signal from thinner samples. Micro - or nano-crystal elect ron diffraction (MicroED) is thus well - suited for the analysis of small crystals, producing high-resolution 3D structures of small chemical compounds or biological macromolecules. MicroED","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"170 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139361735","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 : 2023-07-07DOI: 10.1107/s2053273323099126
Robert P. Hayes, Edward DiNunzio, Mahdieh Yazdani, Justyna Sikorska, Yili Chen, S. Tyagarajan, Younghee Park, Amy Lee, Cesar Reyes, Daniel Burschowsky, Matthias Zebisch, Yangsi Ou, Marina Bukhtiyarova, Shahriar Niroomand, Yuan Tian, Shawn J. Stachel, Hua Su, Jacqueline D. Hicks, Daniel F. Wyss
,
,
{"title":"Fragment-based screening approach reveals non-orthosteric pockets in the search for allosteric inhibitors of tau-tubulin kinase 1","authors":"Robert P. Hayes, Edward DiNunzio, Mahdieh Yazdani, Justyna Sikorska, Yili Chen, S. Tyagarajan, Younghee Park, Amy Lee, Cesar Reyes, Daniel Burschowsky, Matthias Zebisch, Yangsi Ou, Marina Bukhtiyarova, Shahriar Niroomand, Yuan Tian, Shawn J. Stachel, Hua Su, Jacqueline D. Hicks, Daniel F. Wyss","doi":"10.1107/s2053273323099126","DOIUrl":"https://doi.org/10.1107/s2053273323099126","url":null,"abstract":",","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"88 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139361908","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 : 2023-07-07DOI: 10.1107/s2053273323097875
Shi Feng, Cody Aplin, Thuy-Tien T. Nguyen, R. Cerione
{"title":"Filament formation drives catalysis of glutaminase","authors":"Shi Feng, Cody Aplin, Thuy-Tien T. Nguyen, R. Cerione","doi":"10.1107/s2053273323097875","DOIUrl":"https://doi.org/10.1107/s2053273323097875","url":null,"abstract":"","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"28 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139361978","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 : 2023-07-07DOI: 10.1107/s2053273323099163
William D. Ratcliff
{"title":"Semi- and self-supervised approaches to space group and Bravais lattice determination","authors":"William D. Ratcliff","doi":"10.1107/s2053273323099163","DOIUrl":"https://doi.org/10.1107/s2053273323099163","url":null,"abstract":"","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"2 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139362001","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 : 2023-07-07DOI: 10.1107/s2053273323098066
Mario Lopez, Ryan Stadel, Efrain E. Rodriguez
{"title":"Magnetic structure analysis of NiPS<sub>3−<i>x</i> </sub>Se<sub> <i>x</i> </sub>","authors":"Mario Lopez, Ryan Stadel, Efrain E. Rodriguez","doi":"10.1107/s2053273323098066","DOIUrl":"https://doi.org/10.1107/s2053273323098066","url":null,"abstract":"","PeriodicalId":6903,"journal":{"name":"Acta Crystallographica Section A Foundations and Advances","volume":"28 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139362010","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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