18 results on '"Johnson JE"'
Search Results
2. Seasonal Variations in Western North Atlantic Remote Marine Aerosol Properties
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Quinn, PK, Bates, TS, Coffman, DJ, Upchurch, L, Johnson, JE, Moore, R, Ziemba, L, Bell, TG, Saltzman, ES, Graff, J, and Behrenfeld, MJ
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Climate Action ,Atmospheric Sciences ,Physical Geography and Environmental Geoscience - Abstract
The impact of ocean ecosystems on marine boundary layer aerosols and clouds has been the subject of much research but remains uncertain. Five experiments were recently conducted in the western North Atlantic to assess if the seasonally recurring phytoplankton bloom affects aerosol properties. These experiments include the second Western Atlantic Climate Study and four North Atlantic Aerosols and Marine Ecosystem Study cruises. Measurements of unheated and heated number size distributions, cloud condensation nucleus (CCN) concentrations, and aerosol composition were used to identify primary and secondary aerosol components that could be related to the state of the bloom. Only periods of clean marine air, as defined by radon, particle number concentrations, aerosol light absorption coefficient, and back trajectories, were included in the analysis. Nonvolatile material was found to be prevalent in the Aitken mode size range after heating to 230°, likely due to downward mixing from the free troposphere. CCN concentrations at 0.1% supersaturation were best correlated (r2 = 0.73) with accumulation mode nss SO4=. Sea spray aerosol was only correlated with CCN during November when bloom accumulation had not yet occurred and dimethylsulfide concentrations were at a minimum. The fraction of CCN attributable to sea spray aerosol was less than 20% during March, May/June, and September, indicating the limited contribution of sea spray aerosol to the CCN population of the western North Atlantic atmosphere. The strongest link between the plankton bloom and aerosol and cloud properties appears to be due to biogenic non-sea salt SO4=.
- Published
- 2019
3. Water balance creates a threshold in soil pH at the global scale
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Slessarev, EW, Lin, Y, Bingham, NL, Johnson, JE, Dai, Y, Schimel, JP, and Chadwick, OA
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Environmental Sciences ,Soil Sciences ,General Science & Technology - Abstract
Soil pH regulates the capacity of soils to store and supply nutrients, and thus contributes substantially to controlling productivity in terrestrial ecosystems. However, soil pH is not an independent regulator of soil fertility-rather, it is ultimately controlled by environmental forcing. In particular, small changes in water balance cause a steep transition from alkaline to acid soils across natural climate gradients. Although the processes governing this threshold in soil pH are well understood, the threshold has not been quantified at the global scale, where the influence of climate may be confounded by the effects of topography and mineralogy. Here we evaluate the global relationship between water balance and soil pH by extracting a spatially random sample (n = 20,000) from an extensive compilation of 60,291 soil pH measurements. We show that there is an abrupt transition from alkaline to acid soil pH that occurs at the point where mean annual precipitation begins to exceed mean annual potential evapotranspiration. We evaluate deviations from this global pattern, showing that they may result from seasonality, climate history, erosion and mineralogy. These results demonstrate that climate creates a nonlinear pattern in soil solution chemistry at the global scale; they also reveal conditions under which soils maintain pH out of equilibrium with modern climate.
- Published
- 2016
4. An updated climatology of surface dimethlysulfide concentrations and emission fluxes in the global ocean
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Lana, A, Bell, TG, Simó, R, Vallina, SM, Ballabrera‐Poy, J, Kettle, AJ, Dachs, J, Bopp, L, Saltzman, ES, Stefels, J, Johnson, JE, and Liss, PS
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Climate Action ,Atmospheric Sciences ,Geochemistry ,Oceanography ,Meteorology & Atmospheric Sciences - Abstract
The potentially significant role of the biogenic trace gas dimethylsulfide (DMS) in determining the Earth's radiation budget makes it necessary to accurately reproduce seawater DMS distribution and quantify its global flux across the sea/air interface. Following a threefold increase of data (from 15,000 to over 47,000) in the global surface ocean DMS database over the last decade, new global monthly climatologies of surface ocean DMS concentration and sea-to-air emission flux are presented as updates of those constructed 10 years ago. Interpolation/extrapolation techniques were applied to project the discrete concentration data onto a first guess field based on Longhurst's biogeographic provinces. Further objective analysis allowed us to obtain the final monthly maps. The new climatology projects DMS concentrations typically in the range of 1-7 nM, with higher levels occurring in the high latitudes, and with a general trend toward increasing concentration in summer. The increased size and distribution of the observations in the DMS database have produced in the new climatology substantially lower DMS concentrations in the polar latitudes and generally higher DMS concentrations in regions that were severely undersampled 10 years ago, such as the southern Indian Ocean. Using the new DMS concentration climatology in conjunction with state-of-the-art parameterizations for the sea/air gas transfer velocity and climatological wind fields, we estimate that 28.1 (17.6-34.4) Tg of sulfur are transferred from the oceans into the atmosphere annually in the form of DMS. This represents a global emission increase of 17% with respect to the equivalent calculation using the previous climatology. This new DMS climatology represents a valuable tool for atmospheric chemistry, climate, and Earth System models. Copyright © 2011 by the American Geophysical Union.
- Published
- 2011
5. Spatial and temporal variability of the dimethylsulfide to chlorophyll ratio in the surface ocean: An assessment based on phytoplankton group dominance determined from space
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Masotti, I, Belviso, S, Alvain, S, Johnson, JE, Bates, TS, Tortell, PD, Kasamatsu, N, Mongin, M, Marandino, CA, Saltzman, ES, and Moulin, C
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Biotechnology ,Meteorology & Atmospheric Sciences ,Earth Sciences ,Environmental Sciences ,Biological Sciences - Abstract
Dimethylsulfoniopropionate (DMSP) is produced in surface seawater by phytoplankton. Phytoplankton culture experiments have shown that nanoeucaryotes (NANO) display much higher mean DMSP-to-Carbon or DMSP-to-Chlorophyll (Chl) ratios than Prochlorococcus (PRO), Synechococcus (SYN) or diatoms (DIAT). Moreover, the DMSP-lyase activity of algae which cleaves DMSP into dimethylsulfide (DMS) is even more group specific than DMSP itself. Ship-based observations have shown at limited spatial scales, that sea surface DMS-to-Chl ratios (DMS:Chl) are dependent on the composition of phytoplankton groups. Here we use satellite remote sensing of Chl (from SeaWiFS) and of Phytoplankton Group Dominance (PGD from PHYSAT) with ship-based sea surface DMS concentrations (8 cruises in total) to assess this dependence on an unprecedented spatial scale. PHYSAT provides PGD (either NANO, PRO, SYN, DIAT, Phaeocystis (PHAEO) or coccolithophores (COC)) in each satellite pixel (1/4° horizontal resolution). While there are identification errors in the PHYSAT method, it is important to note that these errors are lowest for NANO PGD which we typify by high DMSP:Chl. In summer, in the Indian sector of the Southern Ocean, we find that mean DMS:Chl associated with NANO + PHAEO and PRO + SYN + DIAT are 13.6±8.4 mmol g-1 (n = 34) and 7.3±4.8 mmol g -1 (n = 24), respectively. That is a statistically significant difference (P
- Published
- 2010
6. BMP11 - A candidate negative regulator of olfactory neurogenesis.
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Wu, HH, Chern, P, Johnson, JE, and Calof, AL
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Developmental Biology ,Biological Sciences ,Medical and Health Sciences - Published
- 2001
7. Direct imaging of interactions between an icosahedral virus and conjugate F(ab) fragments by cryoelectron microscopy and X-ray crystallography.
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Porta, C, Wang, G, Cheng, H, Chen, Z, Baker, TS, and Johnson, JE
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Animals ,Mice ,Inbred BALB C ,Rabbits ,Mice ,Comovirus ,Immunoglobulin G ,Antibodies ,Monoclonal ,Binding Sites ,Antibody ,Microscopy ,Electron ,Enzyme-Linked Immunosorbent Assay ,Crystallography ,X-Ray ,Immunoglobulin Fab Fragments ,Good Health and Well Being ,Biological Sciences ,Agricultural and Veterinary Sciences ,Medical and Health Sciences ,Virology - Abstract
The binding properties of seven mouse monoclonal antibodies (McAbs) raised against cowpea mosaic virus (CPMV) were characterized by conventional and inhibition enzyme-linked immunosorbent assay (ELISA) technique. McAb binding to CPMV on electron microscope (EM) grids was also assayed with gold-labeled anti-mouse antibodies. Two of the seven McAbs (5B2 and 10B7) were found to bind tighter to CPMV than the others in the inhibition ELISA and the EM assay. F(ab) fragments from both of these McAbs were prepared and complexed with CPMV in solution. Electron micrographs of flash frozen (vitrified) samples of native CPMV and CPMV complexed with F(ab) fragments from McAbs 5B2 and 10B7 as well as IgGs from 5B2 were recorded and reconstructions were computed at 23 A resolution for the CPMV/F(ab) complexes and 30 A resolution for the CPMV/IgG complex. Structures of all three complexes clearly displayed the F(ab) fragments distributed with icosahedral symmetry on the surface of CPMV. The IgG bound in a monodentate fashion with only one F(ab) attached to the virus surface. F(ab) fragments from 5B2 and 10B7 bound to nearly identical positions. The refined 2.8 A X-ray structure of CPMV was used to identify the roughly 30 amino acids covered by the F(ab) fragments. The "footprint" spans a subunit interface and appears spatially similar to antigenic site 3B on poliovirus. In a previous, preliminary report of the CPMV/F(ab) 5B2 complex (Wang et al., 1992, Nature 355, 275-278) the wrong enantiomorph of the reconstruction was chosen. This was corrected and, since the F(ab) binds close to a mirror plane, the change in the footprint was minor.
- Published
- 1994
8. Functional implications of quasi-equivalence in a T = 3 icosahedral animal virus established by cryo-electron microscopy and X-ray crystallography.
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Cheng, RH, Reddy, VS, Olson, NH, Fisher, AJ, Baker, TS, and Johnson, JE
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Insect Viruses ,Picornaviridae ,Capsid ,Receptors ,Virus ,RNA ,Viral ,Microscopy ,Electron ,Crystallography ,X-Ray ,Nucleic Acid Conformation ,Protein Conformation ,Freezing ,Models ,Molecular ,CRYOELECTRON MICROSCOPY ,NODAVIRUSES ,RNA-PROTEIN INTERACTIONS ,QUASI-EQUIVALENCE ,VIRAL INFECTION ,Infectious Diseases ,Infection ,Chemical Sciences ,Biological Sciences ,Information and Computing Sciences ,Biophysics - Abstract
BackgroundStudies of simple RNA animal viruses show that cell attachment, particle destabilization and cell entry are complex processes requiring a level of capsid sophistication that is difficult to achieve with a shell containing only a single gene product. Nodaviruses [such as Flock House virus (FHV)] are an exception. We have previously determined the structure of FHV at 3 A resolution, and now combine this information with data from cryo-electron microscopy in an attempt to clarify the process by which nodaviruses infect animal cells.ResultsA difference map was computed in which electron density at 22 A resolution, derived from the 3.0 A resolution X-ray model of the FHV capsid protein, was subtracted from the electron density derived from the cryo-electron microscopy reconstruction of FHV at 22 A resolution. Comparisons of this density with the X-ray model showed that quasi-equivalent regions of identical polypeptide sequences have markedly different interactions with the bulk RNA density. Previously reported biphasic kinetics of particle maturation and the requirement of subunit cleavage for particle infectivity are consistent with these results.ConclusionsOn the basis of this study we propose a model for nodavirus infection that is conceptually similar to that proposed for poliovirus but differs from it in detail. The constraints of a single protein type in the capsid lead to a noteworthy use of quasi-symmetry not only to control the binding of a 'pocket factor' but also to modulate maturation cleavage and to release a pentameric helical bundle (with genomic RNA attached) that may further interact with the cell membrane.
- Published
- 1994
9. The comparison of instrumentation for tropospheric measurements of dimethyl sulfide: aircraft results for concentrations at the parts-per-trillion level
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Saltzman, ES, Gregory, GL, Warren, LS, Andreae, MO, Bandy, AR, Ferek, RJ, and Johnson, JE
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- 1994
10. Comparative studies of T = 3 and T = 4 icosahedral RNA insect viruses
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Johnson, JE, Munshi, S, Liljas, L, Agrawal, D, Olson, NH, Reddy, V, Fisher, A, McKinney, B, Schmidt, T, and Baker, TS
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Biochemistry and Cell Biology ,Chemical Sciences ,Biological Sciences ,Crystallography ,X-Ray ,Insect Viruses ,Microscopy ,Electron ,Models ,Molecular ,Models ,Structural ,Molecular Conformation ,RNA Viruses ,Virology - Abstract
Crystallographic and molecular biological studies of T = 3 nodaviruses (180 identical subunits in the particle) and T = 4 tetraviruses (240 identical subunits in the particle) have revealed similarity in both the architecture of the particles and the strategy for maturation. The comparative studies provide a novel opportunity to examine an apparent evolution of particle size, from smaller (T = 3) to larger (T = 4), with both particles based on similar subunits. The BBV and FHV nodavirus structures are refined at 2.8 A and 3 A respectively, while the N omega V structure is at 6 A resolution. Nevertheless, the detailed comparisons of the noda and tetravirus X-ray electron density maps show that the same type of switching in subunit twofold contacts is used in the T = 3 and T = 4 capsids, although differences must exist between quasi and icosahedral threefold contacts in the T = 4 particle that have not yet been detected. The analyses of primary and tertiary structures of noda and tetraviruses show that N omega V subunits undergo a post assembly cleavage like that observed in nodaviruses and that the cleaved 76 C-terminal residues remain associated with the particle.
- Published
- 1994
11. Preliminary X-ray data analysis of crystalline cowpea chlorotic mottle virus.
- Author
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Speir, JA, Munshi, S, Baker, TS, and Johnson, JE
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Plant Viruses ,RNA Viruses ,Virion ,Crystallization ,X-Ray Diffraction ,Image Processing ,Computer-Assisted ,Biological Sciences ,Agricultural and Veterinary Sciences ,Medical and Health Sciences ,Virology - Abstract
Crystals of cowpea chlorotic mottle virus (CCMV) that diffract X-rays to 3.1 A resolution were grown in a succinate-PEG solution buffered at pH 3.3. The crystals are in space group P2(1)2(1)2(1) with unit cell dimensions of a = 381.26 A, b = 381.26 A, and c = 408.59 A. Four particles occupy the unit cell, placing a single virion in the crystallographic asymmetric unit. Diffraction intensities measured from 196 films collected at the Cornell High Energy Synchrotron Source accounted for 55% of the theoretically possible data to 3.2 A. Unit cell dimensions and rotation function analyses of the X-ray data revealed that the particles were organized in a pseudo-tetragonal relationship with the pseudo-fourfold axis along the crystal c axis. Analysis of electron micrographs of two-dimensional crystals of CCMV revealed a remarkable similarity between these and planes of particles perpendicular to the crystallographic c axis in the three-dimensional crystal.
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- 1993
12. Ozone observations and a model of marine boundary layer photochemistry during SAGA 3
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Thompson, AM, Johnson, JE, Torres, AL, Bates, TS, Kelly, KC, Atlas, E, Greenberg, JP, Donahue, NM, Yvon, SA, Saltzman, ES, Heikes, BG, Mosher, BW, Shashkov, AA, and Yegorov, VI
- Published
- 1993
13. The three-dimensional structure of frozen-hydrated Nudaurelia capensis β Virus, a T = 4 insect Virus
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Olson, NH, Baker, TS, Johnson, JE, and Hendry, DA
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Biochemistry and Cell Biology ,Biological Sciences ,Animals ,Capsid ,Freezing ,Image Processing ,Computer-Assisted ,Insect Viruses ,Microscopy ,Electron ,Moths ,Organometallic Compounds ,RNA Viruses ,RNA ,Viral ,Staining and Labeling ,Viral Proteins ,Water ,Zoology ,Biophysics ,Biochemistry and cell biology - Abstract
The three-dimensional structure of Nudaurelia capensis beta virus (N beta V) was reconstructed to 3.2-nm resolution from images of frozen-hydrated virions. The distinctly icosahedral capsid (approximately 40-nm diameter) contains 240 copies of a single 61-kDa protein subunit arranged with T = 4 lattice symmetry. The outer surface of unstained virions compares remarkably well with that previously observed in negatively stained specimens. Inspection of the density map, volume estimates, and model building experiments indicate that each subunit consists of two distinct domains. The large domain (approximately 40 kDa) has a cylindrical shape, approximately 4-nm diameter by approximately 4-nm high, and associates with two large domains of neighboring subunits to form a Y-shaped trimeric aggregate in the outer capsid surface. Four trimers make up each of the 20 planar faces of the capsid. Small domains (approximately 21 kDa) presumably associate at lower radii (approximately 13-16.5 nm) to form a contiguous, non-spherical shell. A T = 4 model, constructed from 80 trimers of the common beta-barrel core motif (approximately 20 kDa) found in many of the smaller T = 3 and pseudo T = 3 viruses, fits the dimensions and features seen in the N beta V reconstruction, suggesting that the contiguous shell of N beta V may be formed by intersubunit contacts between small domains having that motif. The small (approximately 1800 kDa), ssRNA genome is loosely packed inside the capsid with a low average density.
- Published
- 1990
14. Dynamic and geometric analyses of Nudaurelia capensis ω virus maturation reveal the energy landscape of particle transitions
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Tang, J, Kearney, BM, Wang, Q, Doerschuk, PC, Baker, TS, and Johnson, JE
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virus maturation ,Protein Structure ,Insecta ,viruses ,variance map ,Biophysics ,Insect Viruses ,maximum likelihood estimation ,Article ,Quaternary ,Capsid ,NV ,autocatalysis ,Animals ,RNA Viruses ,virus capsid quasi-equivalence ,virus particle dynamics ,Protein Structure, Quaternary ,Virion ,biochemical phenomena, metabolism, and nutrition ,Virus Latency ,Insects ,cryoEM ,Chemical Sciences ,NωV - Abstract
Quasi-equivalent viruses that infect animals and bacteria require a maturation process in which particles transition from initially assembled procapsids to infectious virions. Nudaurelia capensis ω virus (NωV) is a T = 4, eukaryotic, single-stranded ribonucleic acid virus that has proved to be an excellent model system for studying the mechanisms of viral maturation. Structures of NωV procapsids (diameter = 480 Å), a maturation intermediate (410 Å), and the mature virion (410 Å) were determined by electron cryo-microscopy and three-dimensional image reconstruction (cryoEM). The cryoEM density for each particle type was analyzed with a recently developed maximum likelihood variance (MLV) method for characterizing microstates occupied in the ensemble of particles used for the reconstructions. The procapsid and the mature capsid had overall low variance (i.e., uniform particle populations) while the maturation intermediate (that had not undergone post-assembly autocatalytic cleavage) had roughly two to four times the variance of the first two particles. Without maturation cleavage, the particles assume a variety of microstates, as the frustrated subunits cannot reach a minimum energy configuration. Geometric analyses of subunit coordinates provided a quantitative description of the particle reorganization during maturation. Superposition of the four quasi-equivalent subunits in the procapsid had an average root mean square deviation (RMSD) of 3 Å while the mature particle had an RMSD of 11 Å, showing that the subunits differentiate from near equivalent environments in the procapsid to strikingly non-equivalent environments during maturation. Autocatalytic cleavage is clearly required for the reorganized mature particle to reach the minimum energy state required for stability and infectivity. Copyright © 2014 John Wiley & Sons, Ltd. The electron cryo-microscopy (cryoEM) structures of the procapsid, a maturation intermediate, and the virion of Nudaurelia capensis ω virus were studied with geometric and maximum likelihood variance methods. Geometry showed that the procapsid subunits are in homogenous environments that differentiate upon maturation. Variance analysis highlighted meta stability and structural frustration of the intermediate when maturation was prematurely terminated by mutation. Copyright © 2014 John Wiley & Sons, Ltd.
- Published
- 2014
15. The three-dimensional structure of frozen-hydrated Nudaurelia capensis beta virus, a T = 4 insect virus
- Author
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Olson, NH, Baker, TS, Johnson, JE, and Hendry, DA
- Subjects
Microscopy ,Staining and Labeling ,Image Processing ,Biophysics ,Water ,Insect Viruses ,Moths ,Electron ,Viral Proteins ,Capsid ,Computer-Assisted ,Freezing ,Organometallic Compounds ,Animals ,RNA Viruses ,RNA ,Viral ,Biochemistry and Cell Biology ,Zoology - Abstract
The three-dimensional structure of Nudaurelia capensis beta virus (N beta V) was reconstructed to 3.2-nm resolution from images of frozen-hydrated virions. The distinctly icosahedral capsid (approximately 40-nm diameter) contains 240 copies of a single 61-kDa protein subunit arranged with T = 4 lattice symmetry. The outer surface of unstained virions compares remarkably well with that previously observed in negatively stained specimens. Inspection of the density map, volume estimates, and model building experiments indicate that each subunit consists of two distinct domains. The large domain (approximately 40 kDa) has a cylindrical shape, approximately 4-nm diameter by approximately 4-nm high, and associates with two large domains of neighboring subunits to form a Y-shaped trimeric aggregate in the outer capsid surface. Four trimers make up each of the 20 planar faces of the capsid. Small domains (approximately 21 kDa) presumably associate at lower radii (approximately 13-16.5 nm) to form a contiguous, non-spherical shell. A T = 4 model, constructed from 80 trimers of the common beta-barrel core motif (approximately 20 kDa) found in many of the smaller T = 3 and pseudo T = 3 viruses, fits the dimensions and features seen in the N beta V reconstruction, suggesting that the contiguous shell of N beta V may be formed by intersubunit contacts between small domains having that motif. The small (approximately 1800 kDa), ssRNA genome is loosely packed inside the capsid with a low average density.
- Published
- 1990
16. Low resolution meets high: towards a resolution continuum from cells to atoms.
- Author
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Baker, TS, Baker, TS, Johnson, JE, Baker, TS, Baker, TS, and Johnson, JE
- Published
- 1996
17. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy.
- Author
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Speir, JA, Speir, JA, Munshi, S, Wang, G, Baker, TS, Johnson, JE, Speir, JA, Speir, JA, Munshi, S, Wang, G, Baker, TS, and Johnson, JE
- Abstract
BackgroundRNA-protein interactions stabilize many viruses and also the nucleoprotein cores of enveloped animal viruses (e.g. retroviruses). The nucleoprotein particles are frequently pleomorphic and generally unstable due to the lack of strong protein-protein interactions in their capsids. Principles governing their structures are unknown because crystals of such nucleoprotein particles that diffract to high resolution have not previously been produced. Cowpea chlorotic mottle virions (CCMV) are typical of particles stabilized by RNA-protein interactions and it has been found that crystals that diffract beyond 4.5 A resolution are difficult to grow. However, we report here the purification of CCMV with an exceptionally mild procedure and the growth of crystals that diffract X-rays to 3.2 A resolution.ResultsThe 3.2 A X-ray structure of native CCMV, an icosahedral (T = 3) RNA plant virus, shows novel quaternary structure interactions based on interwoven carboxyterminal polypeptides that extend from canonical capsid beta-barrel subunits. Additional particle stability is provided by intercapsomere contacts between metal ion mediated carboxyl cages and by protein interactions with regions of ordered RNA. The structure of a metal-free, swollen form of the virus was determined by cryo-electron microscopy and image reconstruction. Modeling of this structure with the X-ray coordinates of the native subunits shows that the 29 A radial expansion is due to electrostatic repulsion at the carboxyl cages and is stopped short of complete disassembly by preservation of interwoven carboxyl termini and protein-RNA contacts.ConclusionsThe CCMV capsid displays quaternary structural interactions that are unique compared with previously determined RNA virus structures. The loosely coupled hexamer and pentamer morphological units readily explain their versatile reassembly properties and the pH and metal ion dependent polymorphism observed in the virions. Association of capsomeres through
- Published
- 1995
18. Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography.
- Author
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Wang, GJ, Wang, GJ, Porta, C, Chen, ZG, Baker, TS, Johnson, JE, Wang, GJ, Wang, GJ, Porta, C, Chen, ZG, Baker, TS, and Johnson, JE
- Abstract
Biological processes frequently require the formation of multi-protein or nucleoprotein complexes. Some of these complexes have been produced in homogeneous form, crystallized, and analysed at high resolution by X-ray crystallography (for example, see refs 1-3). Most, however, are too large or too unstable to crystallize. Individual components of such complexes can often be purified and analysed by crystallography. Here we report how the coordinated application of cryoelectron microscopy, three-dimensional image reconstruction, and X-ray crystallography provides a powerful approach to study large, unstable macromolecular complexes. Three-dimensional reconstructions of native cowpea mosaic virus (CMPV) and a complex of CPMV saturated with a Fab fragment of a monoclonal antibody against the virus have been determined at 23 A resolution from low-irradiation images of unstained, frozen-hydrated samples. Despite the nominal resolution of the complex, the physical footprint of the Fab on the capsid surface and the orientation and position of the Fab have been determined to within a few ångstroms by fitting atomic models of CPMV4 and Fab (Kol)5 to reconstructed density maps.
- Published
- 1992
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