Search Results - (Author, Cooperation:J. Coe)
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1Y. Kang ; X. E. Zhou ; X. Gao ; Y. He ; W. Liu ; A. Ishchenko ; A. Barty ; T. A. White ; O. Yefanov ; G. W. Han ; Q. Xu ; P. W. de Waal ; J. Ke ; M. H. Tan ; C. Zhang ; A. Moeller ; G. M. West ; B. D. Pascal ; N. Van Eps ; L. N. Caro ; S. A. Vishnivetskiy ; R. J. Lee ; K. M. Suino-Powell ; X. Gu ; K. Pal ; J. Ma ; X. Zhi ; S. Boutet ; G. J. Williams ; M. Messerschmidt ; C. Gati ; N. A. Zatsepin ; D. Wang ; D. James ; S. Basu ; S. Roy-Chowdhury ; C. E. Conrad ; J. Coe ; H. Liu ; S. Lisova ; C. Kupitz ; I. Grotjohann ; R. Fromme ; Y. Jiang ; M. Tan ; H. Yang ; J. Li ; M. Wang ; Z. Zheng ; D. Li ; N. Howe ; Y. Zhao ; J. Standfuss ; K. Diederichs ; Y. Dong ; C. S. Potter ; B. Carragher ; M. Caffrey ; H. Jiang ; H. N. Chapman ; J. C. Spence ; P. Fromme ; U. Weierstall ; O. P. Ernst ; V. Katritch ; V. V. Gurevich ; P. R. Griffin ; W. L. Hubbell ; R. C. Stevens ; V. Cherezov ; K. Melcher ; H. E. Xu
Nature Publishing Group (NPG)
Published 2015Staff ViewPublication Date: 2015-07-23Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Arrestin/*chemistry/*metabolism ; Binding Sites ; Crystallography, X-Ray ; Disulfides/chemistry/metabolism ; Humans ; Lasers ; Mice ; Models, Molecular ; Multiprotein Complexes/biosynthesis/chemistry/metabolism ; Protein Binding ; Reproducibility of Results ; Rhodopsin/*chemistry/*metabolism ; Signal Transduction ; X-RaysPublished by: -
2Staff View
Publication Date: 2011-11-15Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsPublished by: -
3K. Ayyer ; O. M. Yefanov ; D. Oberthur ; S. Roy-Chowdhury ; L. Galli ; V. Mariani ; S. Basu ; J. Coe ; C. E. Conrad ; R. Fromme ; A. Schaffer ; K. Dorner ; D. James ; C. Kupitz ; M. Metz ; G. Nelson ; P. L. Xavier ; K. R. Beyerlein ; M. Schmidt ; I. Sarrou ; J. C. Spence ; U. Weierstall ; T. A. White ; J. H. Yang ; Y. Zhao ; M. Liang ; A. Aquila ; M. S. Hunter ; J. S. Robinson ; J. E. Koglin ; S. Boutet ; P. Fromme ; A. Barty ; H. N. Chapman
Nature Publishing Group (NPG)
Published 2016Staff ViewPublication Date: 2016-02-13Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Crystallization ; Crystallography, X-Ray/*methods ; Models, Molecular ; Photosystem II Protein Complex/*chemistryPublished by: -
4J. Tenboer ; S. Basu ; N. Zatsepin ; K. Pande ; D. Milathianaki ; M. Frank ; M. Hunter ; S. Boutet ; G. J. Williams ; J. E. Koglin ; D. Oberthuer ; M. Heymann ; C. Kupitz ; C. Conrad ; J. Coe ; S. Roy-Chowdhury ; U. Weierstall ; D. James ; D. Wang ; T. Grant ; A. Barty ; O. Yefanov ; J. Scales ; C. Gati ; C. Seuring ; V. Srajer ; R. Henning ; P. Schwander ; R. Fromme ; A. Ourmazd ; K. Moffat ; J. J. Van Thor ; J. C. Spence ; P. Fromme ; H. N. Chapman ; M. Schmidt
American Association for the Advancement of Science (AAAS)
Published 2014Staff ViewPublication Date: 2014-12-06Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Bacterial Proteins/chemistry/*ultrastructure ; Crystallography, X-Ray/*methods ; Photoreceptors, Microbial/chemistry/*ultrastructure ; Protein Conformation ; Time FactorsPublished by: -
5L. A. T. C. Fermi ; M. Ackermann ; M. Ajello ; J. Ballet ; G. Barbiellini ; D. Bastieri ; A. Belfiore ; R. Bellazzini ; B. Berenji ; R. D. Blandford ; E. D. Bloom ; E. Bonamente ; A. W. Borgland ; J. Bregeon ; M. Brigida ; P. Bruel ; R. Buehler ; S. Buson ; G. A. Caliandro ; R. A. Cameron ; P. A. Caraveo ; E. Cavazzuti ; C. Cecchi ; O. Celik ; E. Charles ; S. Chaty ; A. Chekhtman ; C. C. Cheung ; J. Chiang ; S. Ciprini ; R. Claus ; J. Cohen-Tanugi ; S. Corbel ; R. H. Corbet ; S. Cutini ; A. de Luca ; P. R. den Hartog ; F. de Palma ; C. D. Dermer ; S. W. Digel ; E. do Couto e Silva ; D. Donato ; P. S. Drell ; A. Drlica-Wagner ; R. Dubois ; G. Dubus ; C. Favuzzi ; S. J. Fegan ; E. C. Ferrara ; W. B. Focke ; P. Fortin ; Y. Fukazawa ; S. Funk ; P. Fusco ; F. Gargano ; D. Gasparrini ; N. Gehrels ; S. Germani ; N. Giglietto ; F. Giordano ; M. Giroletti ; T. Glanzman ; G. Godfrey ; I. A. Grenier ; J. E. Grove ; S. Guiriec ; D. Hadasch ; Y. Hanabata ; A. K. Harding ; M. Hayashida ; E. Hays ; A. B. Hill ; R. E. Hughes ; G. Johannesson ; A. S. Johnson ; T. J. Johnson ; T. Kamae ; H. Katagiri ; J. Kataoka ; M. Kerr ; J. Knodlseder ; M. Kuss ; J. Lande ; F. Longo ; F. Loparco ; M. N. Lovellette ; P. Lubrano ; M. N. Mazziotta ; J. E. McEnery ; P. F. Michelson ; W. Mitthumsiri ; T. Mizuno ; C. Monte ; M. E. Monzani ; A. Morselli ; I. V. Moskalenko ; S. Murgia ; T. Nakamori ; M. Naumann-Godo ; J. P. Norris ; E. Nuss ; M. Ohno ; T. Ohsugi ; A. Okumura ; N. Omodei ; E. Orlando ; M. Ozaki ; D. Paneque ; D. Parent ; M. Pesce-Rollins ; M. Pierbattista ; F. Piron ; G. Pivato ; T. A. Porter ; S. Raino ; R. Rando ; M. Razzano ; A. Reimer ; O. Reimer ; S. Ritz ; R. W. Romani ; M. Roth ; P. M. Saz Parkinson ; C. Sgro ; E. J. Siskind ; G. Spandre ; P. Spinelli ; D. J. Suson ; H. Takahashi ; T. Tanaka ; J. G. Thayer ; J. B. Thayer ; D. J. Thompson ; L. Tibaldo ; M. Tinivella ; D. F. Torres ; G. Tosti ; E. Troja ; Y. Uchiyama ; T. L. Usher ; J. Vandenbroucke ; G. Vianello ; V. Vitale ; A. P. Waite ; B. L. Winer ; K. S. Wood ; M. Wood ; Z. Yang ; S. Zimmer ; M. J. Coe ; F. Di Mille ; P. G. Edwards ; M. D. Filipovic ; J. L. Payne ; J. Stevens ; M. A. Torres
American Association for the Advancement of Science (AAAS)
Published 2012Staff ViewPublication Date: 2012-01-17Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsPublished by: -
6Keim, E. R. ; Polak, M. L. ; Owrutsky, J. C. ; Coe, J. V. ; Saykally, R. J.
College Park, Md. : American Institute of Physics (AIP)
Published 1990Staff ViewISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyNotes: The technique of direct laser absorption spectroscopy in fast ion beams has been employed for the determination of absolute integrated band intensities (S0v) for the ν3 fundamental bands of H3O+ and NH+4. In addition, the absolute band intensities for the ν1 fundamental bands of HN+2 and HCO+ have been remeasured. The values obtained in units of cm−2 atm−1 at STP are 1880(290) and 580(90) for the ν1 fundamentals of HN+2 and HCO+, respectively; and 4000(800) and 1220(190) for the ν3 fundamentals of H3O+ and NH+4, respectively. Comparisons with ab initio results are presented.Type of Medium: Electronic ResourceURL: -
7Coe, J. V. ; Lee, G. H. ; Eaton, J. G. ; Arnold, S. T. ; Sarkas, H. W. ; Bowen, K. H. ; Ludewigt, C. ; Haberland, H. ; Worsnop, D. R.
College Park, Md. : American Institute of Physics (AIP)
Published 1990Staff ViewISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyType of Medium: Electronic ResourceURL: -
8Coe, J. V. ; Owrutsky, J. C. ; Keim, E. R. ; Agman, N. V. ; Hovde, D. C. ; Saykally, R. J.
College Park, Md. : American Institute of Physics (AIP)
Published 1989Staff ViewISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyNotes: We report the development of a new general technique for measuring vibration–rotation spectra of molecular ions with sub-Doppler resolution and with accurate determination of the mass and number density of the carriers of all spectral features. With this method, called direct laser absorption spectroscopy in fast ion beams (DLASFIB), we have carried out the first observation of direct absorption of photons by ions in a fast ion beam. Hyperfine-resolved vibration–rotation transitions of HF+ have been measured, and along with optical combination differences and laser magnetic resonance data, have been analyzed to yield the fluorine hyperfine parameters a, b, c and d for both v=0 and v=1 in the X 2Π state. Comparisons with many-body perturbation theory results are presented.Type of Medium: Electronic ResourceURL: -
9Staff View
ISSN: 1089-7623Source: AIP Digital ArchiveTopics: PhysicsElectrical Engineering, Measurement and Control TechnologyNotes: A mechanically and electronically simple device for recording time-of-flight mass spectra with continuous (cw) ion sources is demonstrated. The principle of operation involves modulation of a cw ion beam by manipulation of beam energy as opposed to deflection across an aperture. The technique works by tagging pulses of ions within a cw ion beam with higher beam energy and separating them from the cw ion beam by virtue of their higher beam energy. Configurations as a mass filter or to record time-of-flight spectra in real time are reported. The technique might find use for mass analysis at the end of an existing cw ion beam or to produce a high-frequency, high-intensity, mass selected, pulsed ion beam at a short distance from a cw ion source.Type of Medium: Electronic ResourceURL: -
10Snodgrass, J. T. ; Coe, J. V. ; Freidhoff, C. B. ; McHugh, K. M. ; Bowen, K. H.
College Park, Md. : American Institute of Physics (AIP)
Published 1988Staff ViewISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyType of Medium: Electronic ResourceURL: -
11Freidhoff, C. B. ; Snodgrass, J. T. ; Coe, J. V. ; McHugh, K. M. ; Bowen, K. H.
College Park, Md. : American Institute of Physics (AIP)
Published 1986Staff ViewISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyType of Medium: Electronic ResourceURL: -
12Coe, J. V. ; Snodgrass, J. T. ; Freidhoff, C. B. ; McHugh, K. M. ; Bowen, K. H.
College Park, Md. : American Institute of Physics (AIP)
Published 1985Staff ViewISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyNotes: The negative ion photoelectron spectrum of the negative cluster ion H− (NH3)1 has been recorded with 2.540 eV photons. This negative cluster ion was prepared in a supersonic nozzle-ion source involving the injection of electrons into an expanding jet. While the spectrum is dominated by a broadened peak centered at 1.430±0.019 eV, there is also a small feature centered at 0.997±0.031 eV. Our interpretation of this spectrum is that the main peak contains the origin of the photodetachment transition, and that the smaller one is due primarily to the excitation of a stretching mode in the ammonia solvent during photodetachment. An upper limit to the dissociation energy of H−(NH3)1 into H− and NH3 is found to be 0.36 eV. This result is in good agreement with calculations by Kalcher, Squires, and Schleyer. The separation between the main and the small peaks is 3490±130 cm−1, and the symmetric stretching frequency of free NH3 is 3506 cm−1. The small peak also shifts appropriately upon deuteration in support of this assignment.Type of Medium: Electronic ResourceURL: -
13Coe, J. V. ; Snodgrass, J. T. ; Freidhoff, C. B. ; McHugh, K. M. ; Bowen, K. H.
College Park, Md. : American Institute of Physics (AIP)
Published 1987Staff ViewISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyNotes: We have recorded the photoelectron (photodetachment) spectra of the gas-phase negative cluster ions NO−(N2 O)1 and NO−(N2 O)2 using 2.540 eV photons. Both spectra exhibit structured photoelectron spectral patterns which strongly resemble that of free NO−, but which are shifted to successively lower electron kinetic energies with their individual peaks broadened. Each of these spectra is interpreted in terms of a largely intact NO−subion which is solvated and stabilized by nitrous oxide. For both NO−(N2 O)1 and NO−(N2 O)2, the ion–solvent dissociation energies for the loss of single N2 O solvent molecules were determined to be ∼0.2 eV. Electron affinities were also determined and found to increase with cluster size. The localization of the cluster ion's excess negative charge onto its nitric oxide rather than its nitrous oxide subunit is discussed in terms of kinetic factors and a possible barrier between the two forms of the solvated ion.Type of Medium: Electronic ResourceURL: -
14Coe, J. V. ; Snodgrass, J. T. ; Freidhoff, C. B. ; McHugh, K. M. ; Bowen, K. H.
College Park, Md. : American Institute of Physics (AIP)
Published 1986Staff ViewISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyNotes: We have recorded the photoelectron spectrum of SeO− using a newly constructed negative ion photoelectron spectrometer. The adiabatic electron affinity of SeO is determined to be 1.456±0.020 eV. Values of ν00(a 1Δ–X 3Σ−0+) and ΔG1/2(a 1Δ) are found to be 5530±200 and 916±35 cm−1, respectively, in substantial accord with previous measurements. The negative ion parameters determined in this work are: B‘e(SeO−) =0.4246±0.0050 cm−1 which leads to r'e(SeO−)=1.726±0.010 A(ring), ω‘e(SeO−)=730±25 cm−1, ω'e x‘e(SeO−)=2±4 cm−1, and D0(SeO−)=3.84±0.09 eV. In addition, the spectroscopic parameters of SeO− are compared with those of the electronically analogous negative ions: O−2, SO−, and S−2.Type of Medium: Electronic ResourceURL: -
15Staff View
ISSN: 1365-3083Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Serum amyloid P protein (SAP) is a ubiquitous vertebrate protein distinguished by its conservative evolution and paucity of polymorphic forms. The SAP homologue in the Syrian hamster (Mesocricetus auratus), called Female Protein [FP(SAP)] is unique because its synthesis is controlled by sex hormones. These observations were limited to the commercially available standard Syrian hamsters that are descendants of three littermates captured in Syria in 1930. The authors examined FP(SAP) expression in nine inbred lines of Syrian hamsters that were derived from 12 wild hamsters captured in 1971. In general, regulation of FP(SAP) was similar in the new wild hamster strains, although a novel electrophoretically slower FP(SAP) was found in three of the strains. The slow FP(SAP) was not distinguished by size, antigenicity, binding capacity, or regulation. The electrophoretic difference was still apparent after deglycosylation. Hybrid offspring coexpressed both fast and slow FP monomers and formed a unique hybrid pentamer that had a new mobility between the fast and slow parent FP(SAP). The origin of this unusual polymorphism could be related to the amyloidogenesis associated with expression of FP(SAP) in the standard Syrian hamster.Type of Medium: Electronic ResourceURL: -
16Coe, J. G. S. ; Murray, L. E. ; Kennedy, C. J. ; Dawes, L W.
Oxford, UK : Blackwell Publishing Ltd
Published 1992Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: A library of random yeast genomic DNA:lacZ fusions has been constructed using an episomal yeast-Escherichia coli shuttle vector (pCS1). Plasmid pCS1 requires insertion of a promoter and an inframe ATG codon upstream of its resident truncated lacZ gene to regulate expression in yeast. Yeast genomic DNA fragments of 4–6 kb were generated by partial digestion with Sau3A and ligated into the unique BamHI site of plasmid pCS1 to generate a library of 5 × 104 individual E. coli transformants. This library was screened to identify promoter-lacZ fusions that were expressed uniquely during sporulation. Of 342 yeast transformants that exhibited β-galactosidase activity, two were found to express the lacZ gene in a sporulation-specific manner.This paper presents the characterization of two genomic yeast DNA fragments containing promoters that control lacZ expression during the sporulation process. Expression from the promoter present in plasmid pJC18 occurred from 11–21 hours into the sporulation process, while the promoter in plasmid pJC217 was active from 4–14 hours. Staining of nuclear DNA to correlate nuclear morphology with timing of gene expression showed when each of these promoters was active in terms of the morphological stages of sporulation.Type of Medium: Electronic ResourceURL: -
17Staff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] As implied by the absence of the word "complex" from the title, this book is not concerned with metal complex ions in general. The author has wisely chosen to focus attention on the properties and certain reactions of metal ions that contain one or more solvent molecules as ligands. In view of the ...Type of Medium: Electronic ResourceURL: -
18Staff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] Most of this study was concerned with Ig in the garter snake (Thamnophis ordinoides). This species has three antigenically distinct serum Ig classes: a 20.5S macroglobulin (called IgM) and two 9S gamma globulins, Ig-1 and Ig-2 (our work in preparation with D. Leong and L. Thomas). Antiserum to ...Type of Medium: Electronic ResourceURL: -
19Staff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] THE first three chapters of this book will be useful to anyone who wishes to acquire a good background knowledge before beginning a study of the complicated hydrolysis equilibria of metal cations. Methods of measurement (chiefly potentiometric) and the interpretation and treatment of data are ...Type of Medium: Electronic ResourceURL: -
20Staff View
ISSN: 0090-6980Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: MedicineType of Medium: Electronic ResourceURL: