A ‘Build and Retrieve’ methodology to simultaneously solve cryo-EM structures of membrane proteins
暂无分享,去创建一个
C. Robinson | C. Su | J. Bolla | E. Yu | C. E. Morgan | M. Lyu
[1] Wei Huang,et al. Cryo-electron Microscopy Structure of the Acinetobacter baumannii 70S Ribosome and Implications for New Antibiotic Development , 2020, mBio.
[2] R. Read,et al. Improvement of cryo-EM maps by density modification , 2019, Nature Methods.
[3] Z. Zhou,et al. Bottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu , 2019, Nature Methods.
[4] G. Lander,et al. High-resolution structure determination of sub-100 kDa complexes using conventional cryo-EM , 2019, Nature Communications.
[5] H. Stahlberg,et al. Microfluidic protein isolation and sample preparation for high-resolution cryo-EM , 2019, Proceedings of the National Academy of Sciences.
[6] David W. Taylor,et al. Electron microscopy snapshots of single particles from single cells , 2018, The Journal of Biological Chemistry.
[7] S. Matthews,et al. Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry , 2018, Science.
[8] Daniel E. Goldberg,et al. Malaria Parasite Translocon Structure and Mechanism of Effector Export , 2018, Nature.
[9] Randy J Read,et al. Real-space refinement in PHENIX for cryo-EM and crystallography , 2018, bioRxiv.
[10] P. Bork,et al. Capturing protein communities by structural proteomics in a thermophilic eukaryote , 2017, Molecular systems biology.
[11] R. Gennis,et al. Location of the Substrate Binding Site of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli. , 2017, Journal of the American Chemical Society.
[12] Nitin Kumar,et al. Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN , 2017, Proceedings of the National Academy of Sciences.
[13] D. Agard,et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy , 2017, Nature Methods.
[14] David J. Fleet,et al. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination , 2017, Nature Methods.
[15] Richard Henderson,et al. Single particle electron cryomicroscopy: trends, issues and future perspective , 2016, Quarterly Reviews of Biophysics.
[16] E. Wagar. Bioterrorism and the Role of the Clinical Microbiology Laboratory , 2015, Clinical Microbiology Reviews.
[17] Erik G Marklund,et al. Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles. , 2015, Analytical chemistry.
[18] G. Palacios,et al. Whole-Genome Assemblies of 56 Burkholderia Species , 2014, Genome Announcements.
[19] D. Newman,et al. Fosmidomycin Decreases Membrane Hopanoids and Potentiates the Effects of Colistin on Burkholderia multivorans Clinical Isolates , 2014, Antimicrobial Agents and Chemotherapy.
[20] H. Schweizer. Mechanisms of antibiotic resistance in Burkholderia pseudomallei: implications for treatment of melioidosis. , 2012, Future microbiology.
[21] Renato J. Alves,et al. The superfamily of heme-copper oxygen reductases: types and evolutionary considerations. , 2012, Biochimica et biophysica acta.
[22] D. Speert,et al. Identification of Hopanoid Biosynthesis Genes Involved in Polymyxin Resistance in Burkholderia multivorans , 2011, Antimicrobial Agents and Chemotherapy.
[23] Maureen L. Coleman,et al. The RND-family transporter, HpnN, is required for hopanoid localization to the outer membrane of Rhodopseudomonas palustris TIE-1 , 2011, Proceedings of the National Academy of Sciences.
[24] R. Gennis,et al. The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli. , 2010, Biochimica et biophysica acta.
[25] R. Jernigan,et al. Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport , 2010, Nature.
[26] Vincent B. Chen,et al. Correspondence e-mail: , 2000 .
[27] Paola Storici,et al. Crystal structure of osmoporin OmpC from E. coli at 2.0 A. , 2006, Journal of molecular biology.
[28] David N Mastronarde,et al. Automated electron microscope tomography using robust prediction of specimen movements. , 2005, Journal of structural biology.
[29] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[30] P. Loewen,et al. Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli. , 2004, Acta crystallographica. Section D, Biological crystallography.
[31] O. White,et al. Structural flexibility in the Burkholderia mallei genome. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[32] H. Nikaido. Molecular Basis of Bacterial Outer Membrane Permeability Revisited , 2003, Microbiology and Molecular Biology Reviews.
[33] M. Grütter,et al. Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase , 2003, The EMBO journal.
[34] S. Iwata,et al. Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation , 2003, Science.
[35] Randy J Read,et al. Electronic Reprint Biological Crystallography Phenix: Building New Software for Automated Crystallographic Structure Determination Biological Crystallography Phenix: Building New Software for Automated Crystallographic Structure Determination , 2022 .
[36] A. Puustinen,et al. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site , 2000, Nature Structural Biology.
[37] A. Shevchenko,et al. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. , 1996, Analytical chemistry.
[38] G. Rummel,et al. Crystal structures explain functional properties of two E. coli porins , 1992, Nature.