{"title":"Current state of automated crystallographic data analysis.","authors":"V S Lamzin, A Perrakis","doi":"10.1038/80763","DOIUrl":"https://doi.org/10.1038/80763","url":null,"abstract":"<p><p>A goal of structural biology--and of structural genomics in particular--is to improve the underlying methodology for high-throughput determination of three-dimensional structures of biological macromolecules. Here we address issues related to the development, automation and streamlining of the process of macromolecular X-ray crystal structure solution.</p>","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"7 Suppl ","pages":"978-81"},"PeriodicalIF":0.0,"publicationDate":"2000-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1038/80763","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21928170","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}
{"title":"Target selection for structural genomics.","authors":"S E Brenner","doi":"10.1038/80747","DOIUrl":"https://doi.org/10.1038/80747","url":null,"abstract":"<p><p>Structural genomics aims to use high-throughput structure determination and computational analysis to provide three-dimensional models of every tractable protein. The process of choosing proteins for experimental structure characterization is known as target selection. In this nomenclature, the targets are regions of proteins to be studied by crystallography or NMR. Selection of the targets is principally a computational process of restricting candidate proteins to those that are tractable and of unknown structure, and prioritizing according to expected interest and accessibility.</p>","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"7 Suppl ","pages":"967-9"},"PeriodicalIF":0.0,"publicationDate":"2000-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1038/80747","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21928167","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}
S Yokoyama, H Hirota, T Kigawa, T Yabuki, M Shirouzu, T Terada, Y Ito, Y Matsuo, Y Kuroda, Y Nishimura, Y Kyogoku, K Miki, R Masui, S Kuramitsu
{"title":"Structural genomics projects in Japan.","authors":"S Yokoyama, H Hirota, T Kigawa, T Yabuki, M Shirouzu, T Terada, Y Ito, Y Matsuo, Y Kuroda, Y Nishimura, Y Kyogoku, K Miki, R Masui, S Kuramitsu","doi":"10.1038/80712","DOIUrl":"https://doi.org/10.1038/80712","url":null,"abstract":"<p><p>Two major structural genomics projects exist in Japan. The oldest, the RIKEN Structural Genomics Initiative, has two major goals: to determine bacterial, mammalian, and plant protein structures by X-ray crystallography and NMR spectroscopy and to perform functional analyses with the target proteins. The newest, the structural genomics project at the Biological Information Research Center, focuses on human membrane proteins.</p>","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"7 Suppl ","pages":"943-5"},"PeriodicalIF":0.0,"publicationDate":"2000-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1038/80712","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21928159","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}
T C Meyers, T A Turano, D A Greenhalgh, P R Waller
{"title":"Patent protection for protein structures and databases.","authors":"T C Meyers, T A Turano, D A Greenhalgh, P R Waller","doi":"10.1038/80723","DOIUrl":"https://doi.org/10.1038/80723","url":null,"abstract":"<p><p>Patent protection is available for certain inventions in the field of structural genomics. A review of the patent application procedure is provided, and patentable aspects of protein structural information under US law are discussed. Strategic and international factors to consider when seeking patent protection for an invention also are presented.</p>","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"7 Suppl ","pages":"950-2"},"PeriodicalIF":0.0,"publicationDate":"2000-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1038/80723","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21928161","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}
A M Edwards, C H Arrowsmith, D Christendat, A Dharamsi, J D Friesen, J F Greenblatt, M Vedadi
{"title":"Protein production: feeding the crystallographers and NMR spectroscopists.","authors":"A M Edwards, C H Arrowsmith, D Christendat, A Dharamsi, J D Friesen, J F Greenblatt, M Vedadi","doi":"10.1038/80751","DOIUrl":"https://doi.org/10.1038/80751","url":null,"abstract":"<p><p>Protein purification efforts for structural genomics will focus on automation for the readily-expressed proteins, and process development for the more difficult ones, such as membrane proteins. Thousands of proteins are expected to be produced in the next few years. The purified proteins will be valuable reagents for the entire research community.</p>","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"7 Suppl ","pages":"970-2"},"PeriodicalIF":0.0,"publicationDate":"2000-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1038/80751","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21928168","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}
R. Sankaranarayanan, A. Dock‐Brégeon, B. Rees, M. Bovee, J. Caillet, P. Romby, C. Francklyn, D. Moras
{"title":"Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase","authors":"R. Sankaranarayanan, A. Dock‐Brégeon, B. Rees, M. Bovee, J. Caillet, P. Romby, C. Francklyn, D. Moras","doi":"10.1038/nsb0600_461","DOIUrl":"https://doi.org/10.1038/nsb0600_461","url":null,"abstract":"","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"35 1","pages":"461-465"},"PeriodicalIF":0.0,"publicationDate":"2000-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84554602","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}
{"title":"Observing conformational and activity changes of tet repressor in vivo.","authors":"B Tiebel, K Garke, W Hillen","doi":"10.1038/75883","DOIUrl":"https://doi.org/10.1038/75883","url":null,"abstract":"<p><p>Effector triggered conformational changes of proteins such as regulators of transcription, receptors, or enzymes are the molecular basis for regulation in biology. Most proteins perform their biological functions intracellularly, in the presence of many potential interaction partners. Studies of conformational changes have mainly been performed in vitro using sophisticated physical and biochemical methods that usually require purified proteins. Here we describe the observation of conformational changes of Tet repressor in the cytoplasm of growing Escherichia coli cells, analyzed by ligand dependent disulfide crosslinking of cysteine residues substituted into mobile regions of the protein. The amount of protein undergoing the structural change is quantitatively linked to the concomitant induction of transcription of a reporter gene.</p>","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"7 6","pages":"479-81"},"PeriodicalIF":0.0,"publicationDate":"2000-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1038/75883","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21723564","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}
{"title":"The SsrA–SmpB system for protein tagging, directed degradation and ribosome rescue","authors":"A. Karzai, E. Roche, R. Sauer","doi":"10.1038/nsb0600_449","DOIUrl":"https://doi.org/10.1038/nsb0600_449","url":null,"abstract":"","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"10 1","pages":"449-455"},"PeriodicalIF":0.0,"publicationDate":"2000-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80867745","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}
J. Ménétrey, E. Macia, S. Pasqualato, M. Franco, J. Cherfils
{"title":"Structure of Arf6–GDP suggests a basis for guanine nucleotide exchange factors specificity","authors":"J. Ménétrey, E. Macia, S. Pasqualato, M. Franco, J. Cherfils","doi":"10.1038/nsb0600_466","DOIUrl":"https://doi.org/10.1038/nsb0600_466","url":null,"abstract":"","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"90 1","pages":"466-469"},"PeriodicalIF":0.0,"publicationDate":"2000-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76202991","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}
M. Irving, G. Piazzesi, L. Lucii, Yin-Biao Sun, J. Harford, I. Dobbie, M. Ferenczi, M. Reconditi, V. Lombardi
{"title":"Conformation of the myosin motor during force generation in skeletal muscle","authors":"M. Irving, G. Piazzesi, L. Lucii, Yin-Biao Sun, J. Harford, I. Dobbie, M. Ferenczi, M. Reconditi, V. Lombardi","doi":"10.1038/nsb0600_482","DOIUrl":"https://doi.org/10.1038/nsb0600_482","url":null,"abstract":"","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"479 1","pages":"482-485"},"PeriodicalIF":0.0,"publicationDate":"2000-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77050081","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}