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1. Full Text Quantitative multicolor subdiffraction imaging of bacterial protein ultrastructures in three dimensions
by Gahlmann, Andreas and Ptacin, Jerod L and Grover, Ginni and Quirin, Sean and Von Diezmann, Alexander R. S and Lee, Marissa K and Backlund, Mikael P and Shapiro, Lucy and Piestun, Rafael and Moerner, W.E
Nano Letters, ISSN 1530-6984, 03/2013, Volume 13, Issue 3, pp. 987 - 993
We demonstrate quantitative multicolor three-dimensional (3D) subdiffraction imaging of the structural arrangement of fluorescent protein fusions in living... 
Fluorescence | 3D imaging | image registration | biophysics | super-resolution | live-cell imaging | PHYSICS, CONDENSED MATTER | PHYSICS, APPLIED | MATERIALS SCIENCE, MULTIDISCIPLINARY | CHEMISTRY, PHYSICAL | NANOSCIENCE & NANOTECHNOLOGY | CHEMISTRY, MULTIDISCIPLINARY | NANOSCOPY | Bacterial Proteins - ultrastructure | Color | Caulobacter crescentus - chemistry | Proteins | Image registration | Algorithms | Wavelengths | Imaging | Bacteria | Dielectrics | Three dimensional
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2. Full Text Tripartite assembly of RND multidrug efflux pumps
by Daury, Laetitia and Orange, François and Taveau, Jean-Christophe and Verchère, Alice and Monlezun, Laura and Gounou, Céline and Marreddy, Ravi K. R and Picard, Martin and Broutin, Isabelle and Pos, Klaas M and Lambert, Olivier
Nature Communications, ISSN 2041-1723, 02/2016, Volume 7, Issue 1, p. 10731
Tripartite multidrug efflux systems of Gram-negative bacteria are composed of an inner membrane transporter, an outer membrane channel and a periplasmic... 
PERIPLASMIC COMPONENT | PHOSPHOLIPID-BILAYER NANODISCS | GRAM-NEGATIVE BACTERIA | TOLC | PSEUDOMONAS-AERUGINOSA | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | ANTIBIOTIC-RESISTANCE | TRANSPORTER ACRB | OUTER-MEMBRANE CHANNEL | Microscopy, Electron, Transmission | Native Polyacrylamide Gel Electrophoresis | Bacterial Outer Membrane Proteins - ultrastructure | Escherichia coli | Escherichia coli Proteins - metabolism | Escherichia coli Proteins - ultrastructure | Lipoproteins - ultrastructure | Nanostructures | Multiprotein Complexes - metabolism | Multiprotein Complexes - ultrastructure | Bacterial Outer Membrane Proteins - metabolism | Membrane Transport Proteins - ultrastructure | Drug Resistance, Multiple, Bacterial | Lipoproteins - metabolism | Membrane Transport Proteins - metabolism | Pseudomonas aeruginosa | Periplasmic Proteins - metabolism | Multidrug Resistance-Associated Proteins - metabolism | Multidrug Resistance-Associated Proteins - ultrastructure | Life Sciences
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3. Full Text Multiscale Structuring of the E. coli Chromosome by Nucleoid-Associated and Condensin Proteins
by Lioy, Virginia S and Cournac, Axel and Marbouty, Martial and Duigou, Stéphane and Mozziconacci, Julien and Espéli, Olivier and Boccard, Frédéric and Koszul, Romain
Cell, ISSN 0092-8674, 02/2018, Volume 172, Issue 4, pp. 771 - 783.e18
As in eukaryotes, bacterial genomes are not randomly folded. Bacterial genetic information is generally carried on a circular chromosome with a single origin... 
SMC | bacteria | MatP | chromatin | Hi-C | genome organization | ORGANIZATION | BACTERIAL CHROMOSOME | DNA-BINDING | 3D GENOME | BACILLUS-SUBTILIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | GENE-EXPRESSION | H-NS | TOPOISOMERASE-IV | MOLECULAR-BASIS | CELL BIOLOGY | Chromosomes, Bacterial - genetics | Chromosomal Proteins, Non-Histone - metabolism | Adenosine Triphosphatases - metabolism | Repressor Proteins - genetics | Escherichia coli Proteins - metabolism | Multiprotein Complexes - genetics | DNA-Binding Proteins - genetics | Escherichia coli K12 - ultrastructure | Chromosomal Proteins, Non-Histone - genetics | DNA-Binding Proteins - metabolism | DNA-Binding Proteins - ultrastructure | Multiprotein Complexes - metabolism | Multiprotein Complexes - ultrastructure | Chromosomes, Bacterial - metabolism | Escherichia coli K12 - metabolism | Chromosomes, Bacterial - ultrastructure | Protein Structure, Quaternary | Escherichia coli Proteins - genetics | Adenosine Triphosphatases - genetics | Adenosine Triphosphatases - ultrastructure | Escherichia coli K12 - genetics | Repressor Proteins - metabolism | Bacteria | Chromatin | Escherichia coli | Genomics | Escherichia coli K12 | Life Sciences | Escherichia coli Proteins | Adenosine Triphosphatases | Multiprotein Complexes | Repressor Proteins | Chromosomal Proteins, Non-Histone | Chromosomes, Bacterial | DNA-Binding Proteins
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4. Full Text Structure of the human 80S ribosome
by Khatter, Heena and Myasnikov, Alexander G and Natchiar, S. Kundhavai and Klaholz, Bruno P
Nature, ISSN 0028-0836, 04/2015, Volume 520, Issue 7549, pp. 640 - 645
Ribosomes are translational machineries that catalyse protein synthesis. Ribosome structures from various species are known at the atomic level, but obtaining... 
ANGSTROM RESOLUTION | TRANSFER-RNA BINDING | BACTERIAL RIBOSOME | MESSENGER-RNA | PARTICLE ELECTRON CRYOMICROSCOPY | CRYSTAL-STRUCTURE | EUKARYOTIC RIBOSOME | MULTIDISCIPLINARY SCIENCES | O HYDROGEN-BONDS | TRANSLATION INITIATION | L1 STALK | Ribosomal Proteins - chemistry | Ribosome Subunits - chemistry | RNA, Transfer - metabolism | Humans | RNA, Ribosomal - chemistry | Ribosomes - chemistry | Models, Molecular | RNA, Ribosomal - metabolism | Ribosomes - metabolism | RNA, Transfer - ultrastructure | Ribosomal Proteins - metabolism | Cryoelectron Microscopy | RNA, Ribosomal - ultrastructure | Ribosomes - ultrastructure | Ribosomal Proteins - ultrastructure | Ribosome Subunits - ultrastructure | RNA, Transfer - chemistry | Binding Sites | Ribosome Subunits - metabolism | Electrons | Proteins | Structure | Observations | Ribosomes | Antibiotics | Molecular structure | Ribosomal DNA | Ligands | Ribonucleic acid--RNA | Molecular weight
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5. Full Text Structural rearrangements of a polyketide synthase module during its catalytic cycle
by Whicher, Jonathan R and Dutta, Somnath and Hansen, Douglas A and Hale, Wendi A and Chemler, Joseph A and Dosey, Annie M and Narayan, Alison R. H and Håkansson, Kristina and Sherman, David H and Smith, Janet L and Skiniotis, Georgios
Nature, ISSN 0028-0836, 2014, Volume 510, Issue 7506, pp. 560 - 564
The polyketide synthase (PKS) mega-enzyme assembly line uses a modular architecture to synthesize diverse and bioactive natural products that often constitute... 
DOMAIN | DESIGN | RECOGNITION | PARTICLE ELECTRON CRYOMICROSCOPY | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | RESOLUTION | CRYO-EM | CHAIN ELONGATION | PIKROMYCIN | REVEALS | Protein Structure, Tertiary | Catalytic Domain | Biocatalysis | Polyketide Synthases - ultrastructure | Acyl Carrier Protein - metabolism | Bacterial Proteins - chemistry | Models, Molecular | Alcohol Oxidoreductases - metabolism | Macrolides - metabolism | Acyltransferases - metabolism | Alcohol Oxidoreductases - ultrastructure | Cryoelectron Microscopy | Acyl Carrier Protein - chemistry | Polyketide Synthases - chemistry | Polyketide Synthases - metabolism | Alcohol Oxidoreductases - chemistry | Acyltransferases - ultrastructure | Bacterial Proteins - metabolism | Streptomyces - enzymology | Acyltransferases - chemistry | Bacterial Proteins - ultrastructure | Acyl Carrier Protein - ultrastructure | Streptomyces | Polyketides | Observations | Health aspects | Protein-protein interactions | Proteins | Fourier transforms | Biosynthesis | Chromatography | Crystal structure
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6. Full Text Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein
by Tenboer, Jason and Basu, Shibom and Zatsepin, Nadia and Pande, Kanupriya and Milathianaki, Despina and Frank, Matthias and Hunter, Mark and Boutet, Sébastien and Williams, Garth J and Koglin, Jason E and Oberthuer, Dominik and Heymann, Michael and Kupitz, Christopher and Conrad, Chelsie and Coe, Jesse and Roy-Chowdhury, Shatabdi and Weierstall, Uwe and James, Daniel and Wang, Dingjie and Grant, Thomas and Barty, Anton and Yefanov, Oleksandr and Scales, Jennifer and Gati, Cornelius and Seuring, Carolin and Srajer, Vukica and Henning, Robert and Schwander, Peter and Fromme, Raimund and Ourmazd, Abbas and Moffat, Keith and Van Thor, Jasper J and Spence, John C. H and Fromme, Petra and Chapman, Henry N and Schmidt, Marius and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Science, ISSN 0036-8075, 12/2014, Volume 346, Issue 6214, pp. 1242 - 1246
Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of... 
ROOM-TEMPERATURE | X-RAY CRYSTALLOGRAPHY | SPECTROSCOPY | MULTIDISCIPLINARY SCIENCES | NANOCRYSTALLOGRAPHY | PHOTOCYCLE | FREE-ELECTRON LASER | LAUE CRYSTALLOGRAPHY | DIFFRACTION | MACROMOLECULAR CRYSTALLOGRAPHY | STRUCTURAL DYNAMICS | Crystallography, X-Ray - methods | Photoreceptors, Microbial - chemistry | Time Factors | Photoreceptors, Microbial - ultrastructure | Bacterial Proteins - chemistry | Protein Conformation | Bacterial Proteins - ultrastructure | Protein research | Research | Crystallography | Protein-protein interactions | Proteins | Photocatalysis | Crystals | BASIC BIOLOGICAL SCIENCES | OTHER INSTRUMENTATION
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7. Full Text Structural basis for the regulated protease and chaperone function of DegP
by Krojer, Tobias and Clausen, Tim and Schäfer, Eva and Ehrmann, Michael and Sawa, Justyna and Saibil, Helen R
Nature, ISSN 0028-0836, 06/2008, Volume 453, Issue 7197, pp. 885 - 890
All organisms have to monitor the folding state of cellular proteins precisely. The heat- shock protein DegP is a protein quality control factor in the... 
SYSTEM | PERIPLASMIC PROTEIN | PORIN | PDZ DOMAINS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | RESOLUTION | OUTER-MEMBRANE BIOGENESIS | ELECTRON-MICROSCOPY | ENVELOPE STRESS-RESPONSE | Escherichia coli - enzymology | Molecular Chaperones - metabolism | Periplasmic Proteins - chemistry | Heat-Shock Proteins - ultrastructure | Bacterial Outer Membrane Proteins - ultrastructure | Heat-Shock Proteins - metabolism | Bacterial Outer Membrane Proteins - chemistry | Models, Molecular | Crystallography, X-Ray | Serine Endopeptidases - chemistry | Structure-Activity Relationship | Molecular Chaperones - chemistry | Protein Folding | Bacterial Outer Membrane Proteins - biosynthesis | Cryoelectron Microscopy | Serine Endopeptidases - ultrastructure | Bacterial Outer Membrane Proteins - metabolism | Protein Structure, Quaternary | Cell Membrane - metabolism | Periplasmic Proteins - metabolism | Serine Endopeptidases - metabolism | Molecular Chaperones - ultrastructure | Periplasmic Proteins - ultrastructure | Heat-Shock Proteins - chemistry | Heat shock proteins | Chemical properties | Research | Structure | Protein folding | Proteases | Enzymes | E coli | Atoms & subatomic particles | Mass spectrometry | Substrates | Crystal structure
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8. Full Text Structural basis of MsbA-mediated lipopolysaccharide transport
by Mi, Wei and Li, Yanyan and Yoon, Sung Hwan and Ernst, Robert K and Walz, Thomas and Liao, Maofu
Nature, ISSN 0028-0836, 09/2017, Volume 549, Issue 7671, pp. 233 - 237
Lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria is critical for the assembly of their cell envelopes. LPS synthesized in the... 
BINDING CASSETTE TRANSPORTER | ABC TRANSPORTER | MOLECULAR-MECHANISM | COMPLEX | RECOGNITION | RESONANCE | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | ALTERNATING ACCESS | DIVERSITY | FLIPPASE | Bacterial Proteins - chemistry | Lipopolysaccharides - metabolism | Adenosine Diphosphate - chemistry | Escherichia coli - cytology | Cell Membrane - chemistry | ATP-Binding Cassette Transporters - chemistry | Biological Transport | Periplasm - metabolism | ATP-Binding Cassette Transporters - metabolism | Protein Domains | Cell Membrane - metabolism | Periplasm - chemistry | Periplasm - ultrastructure | Nanostructures - ultrastructure | Escherichia coli - enzymology | Models, Molecular | Cell Membrane - ultrastructure | Cryoelectron Microscopy | ATP-Binding Cassette Transporters - ultrastructure | Hydrophobic and Hydrophilic Interactions | Nanostructures - chemistry | Protein Binding | Bacterial Proteins - metabolism | Bacterial Proteins - ultrastructure | Adenosine Diphosphate - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Escherichia coli - ultrastructure | Biological research | Biological transport | Physiological aspects | Cell membranes | Research | Lipopolysaccharides | Biology, Experimental | Lipids | Hydrophobicity | Electron microscopy | ADP | Vanadate | Proteins | Transmission electron microscopy | Bacteria | Transmembrane domains | Gram-negative bacteria | Embedded structures | Cell envelopes | Transporter | Adenosine triphosphate | Conformation | Structural analysis
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9. Full Text Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ
by Maria A. Schumacher and Wenjie Zeng
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2016, Volume 113, Issue 18, pp. 4988 - 4993
Cell division in most prokaryotes is mediated by FtsZ, which polymerizes to create the cytokinetic Z ring. Multiple FtsZ-binding proteins regulate FtsZ... 
Cell division | Nucleoid occlusion | SlmA | FtsZ | Protein-protein interaction | SUPERRESOLUTION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | cell division | ZIPA | SEGREGATION | TO-POLE OSCILLATION | TOPOREGULATION | CELL-DIVISION | BACTERIAL CYTOKINESIS | nucleoid occlusion | RING FORMATION | protein-protein interaction | ASSEMBLY DYNAMICS | Protein Subunits | Chromosome Segregation | Carrier Proteins - ultrastructure | Models, Chemical | Chromosomes, Bacterial - chemistry | Bacterial Proteins - chemistry | Escherichia coli Proteins - ultrastructure | DNA, Bacterial - chemistry | Cytoskeletal Proteins - chemistry | DNA, Bacterial - ultrastructure | DNA-Binding Proteins - chemistry | Cytoskeletal Proteins - ultrastructure | DNA-Binding Proteins - ultrastructure | Chromosomes, Bacterial - ultrastructure | Protein Binding | Protein Domains | Carrier Proteins - chemistry | Protein Conformation | Bacterial Proteins - ultrastructure | Molecular Docking Simulation | Escherichia coli Proteins - chemistry | Nucleic Acid Conformation | Binding Sites | Cellular proteins | Cell research | Physiological aspects | Cytoskeleton | Genetic aspects | Research | Structure | Protein-protein interactions | Proteins | Polymerization | E coli | Prokaryotes | Binding sites | Deoxyribonucleic acid--DNA | protein–protein interaction | Biological Sciences
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10. Full Text Direct Visualization by Cryo-EM of the Mycobacterial Capsular Layer: A Labile Structure Containing ESX-1-Secreted Proteins
by Sani, M and Houben, E.N.G and Geurtsen, J and Pierson, J and De Punder, K and Van Zon, M and Wever, B and Piersma, S.R and Jiménez, C.R and Peters, P.J
Plos Pathogens, 6 (3), 2010, ISSN 1553-7366, 03/2010, Volume 6, Issue 3, p. e1000794
The cell envelope of mycobacteria, a group of Gram positive bacteria, is composed of a plasma membrane and a Gramnegative-like outer membrane containing... 
OUTER-MEMBRANE | TUBERCULOSIS | ESCHERICHIA-COLI | ELECTRON-MICROSCOPY | MICROBIOLOGY | FROZEN-HYDRATED SECTIONS | IN-VITRO | CELL-WALL | VIROLOGY | BOVIS BCG | SECRETION SYSTEM | SURFACE | PARASITOLOGY | Mycobacterium marinum - ultrastructure | Cytokines - metabolism | Mycobacterium smegmatis - metabolism | Bacterial Capsules - metabolism | Bacterial Outer Membrane Proteins - ultrastructure | Humans | Mycobacterium tuberculosis - ultrastructure | Microscopy, Immunoelectron | Mycobacterium bovis - ultrastructure | Cryoelectron Microscopy | Mycobacterium - metabolism | Macrophages - metabolism | Bacterial Outer Membrane Proteins - metabolism | Mycobacterium bovis - metabolism | Mycobacterium smegmatis - ultrastructure | Mycobacterium - ultrastructure | Bacterial Capsules - ultrastructure | Bacterial Outer Membrane Proteins - secretion | Mycobacterium marinum - metabolism | Mycobacterium tuberculosis - metabolism | Macrophages - immunology | Macrophages - microbiology | Mycobacterium | Usage | Cytokines | Bacterial proteins | Mycobacteria | Physiological aspects | Research | Structure | Electron microscopy | Health aspects | Proteins | Microbiology | Microscopy | Bacteria | Lipids | Vaccines | Experiments | Bacteriology
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11. Full Text RNA Targeting by the Type III-A CRISPR-Cas Csm Complex of Thermus thermophilus
by Staals, Raymond H.J and Zhu, Yifan and Taylor, David W and Kornfeld, Jack E and Sharma, Kundan and Barendregt, Arjan and Koehorst, Jasper J and Vlot, Marnix and Neupane, Nirajan and Varossieau, Koen and Sakamoto, Keiko and Suzuki, Takehiro and Dohmae, Naoshi and Yokoyama, Shigeyuki and Schaap, Peter J and Urlaub, Henning and Heck, Albert J.R and Nogales, Eva and Doudna, Jennifer A and Shinkai, Akeo and van der Oost, John
Molecular Cell, ISSN 1097-2765, 11/2014, Volume 56, Issue 4, pp. 518 - 530
CRISPR-Cas is a prokaryotic adaptive immune system that provides sequence-specific defense against foreign nucleic acids. Here we report the structure and... 
ADAPTIVE IMMUNITY | ANTIVIRAL DEFENSE | PROTEIN | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SEED SEQUENCE | GUIDED SURVEILLANCE COMPLEX | BACTERIAL IMMUNE-SYSTEM | HALOFERAX-VOLCANII | MASS-SPECTROMETRY | CELL BIOLOGY | Amino Acid Sequence | CRISPR-Associated Proteins - chemistry | Endoribonucleases - chemistry | Thermus thermophilus - enzymology | Endoribonucleases - ultrastructure | Endoribonucleases - metabolism | Bacterial Proteins - chemistry | Models, Molecular | Molecular Sequence Data | RNA Cleavage | Microscopy, Electron | CRISPR-Associated Proteins - ultrastructure | Thermus thermophilus - genetics | Base Sequence | CRISPR-Associated Proteins - metabolism | Clustered Regularly Interspaced Short Palindromic Repeats | Protein Structure, Quaternary | Protein Binding | RNA, Bacterial - genetics | Bacterial Proteins - metabolism | Bacterial Proteins - ultrastructure | RNA, Bacterial - metabolism | Crosslinked polymers | Architecture | RNA | Mass spectrometry | crystal-structure | mass-spectrometry | bacterial immune-system | protein | guided surveillance complex | escherichia-coli | seed sequence | haloferax-volcanii | antiviral defense | adaptive immunity
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