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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy Section 46 (1990), S. 277-283 
    ISSN: 0584-8539
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy Section 46 (1990), S. 295-301 
    ISSN: 0584-8539
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Magnetic Resonance (1969) 95 (1991), S. 589-596 
    ISSN: 0022-2364
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Magnetic Resonance (1969) 94 (1991), S. 20-33 
    ISSN: 0022-2364
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Magnetic Resonance (1969) 91 (1991), S. 128-135 
    ISSN: 0022-2364
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 27 (1994), S. 868-877 
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The point-spread functions (PSFs) of two X-ray CCD detectors and two imaging-plate (IP) scanners were compared using the monochromatic beam of the Materials Science beamline of the ESRF. The CCD detectors were a commercial medical type X-ray image intensifier (XRII) for energies above 20 keV and a tube with a beryllium window especially designed for the 5–50 keV range, optically coupled to a high-resolution cooled charge-coupled-device (CCD) camera. The IP scanners were the Fuji BAS2000 and the Molecular Dynamics PhosphorImager 400E, with plates from Fuji and Kodak. The PSFs were recorded using a 30 × 30 μm pinhole at energies from 8 to 41 keV under normal and highly saturated conditions. Special care was taken in the study of PSF wings. Dynamic range capabilities in the presence of PSF bleeding were also measured using a standard X-ray generator. The Fuji and MD IP scanners give very similar PSFs when used with Fuji plates [ca 130 μm full width at half-maximum (FWHM), 1100 μm at 0.1% of peak maximum]. The Kodak plates showed a broader PSF than the Fuji plates, one which also increases with X-ray energy. The standard XRII/CCD gave the coarsest PSF (ca 4000 μm at 0.1% of peak maximum), whereas the finest PSF was recorded with the beryllium XRII/CCD used in magnified mode (900 μm at 0.1%). The best dynamic range was obtained with the XRII/CCDs; the lowest with the Fuji scanner.
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  • 7
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 31 (1998), S. 22-35 
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: New software for the integration of weak and/or spatially overlapped diffraction patterns is presented. The program, named PROW (profile fitting for overlapped and weak data), uses box integration with an optimized summation area for strong nonoverlapped spots, and profile fitting with an optimized fitting area for weak and/or overlapped spots. The sizes of the integration areas are dynamically adjusted to find the best compromise between minimal bias resulting from statistical fluctuations of the X-ray background and maximal use of the information content in each diffraction spot. Deconvolution of spatially overlapped spots is performed by a standard least-squares procedure. The program is compatible with the Daresbury Laue software suite and with the DENZO package. It has been tested on several data-sets recorded on image-plate and CCD (charge-coupled device) detectors. Intensities extracted from very weak Laue data-sets containing as many as 60% overlapped spots were shown to be of sufficient quality to lead to an accurate structure refinement. Difficult monochromatic data-sets were also processed successfully, leading to a generally better compromise between reliability factors, redundancy and completeness than previously achieved. Concomitant improvement in atomic model refinement was also observed.
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  • 8
    Electronic Resource
    Electronic Resource
    Chester : International Union of Crystallography (IUCr)
    Journal of synchrotron radiation 3 (1996), S. 65-74 
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Laue diffraction patterns with an exposure time of ca 60 ps have been acquired at the European Synchrotron Radiation Facility (ESRF) on protein crystals by using the single-bunch mode of the storage ring. A 10 ns laser pulse initiating photodissociation was synchronized with the X-ray pulse. The potential for a quantitative detection of conformational changes in proteins on the nanosecond timescale with this technique is demonstrated using the example of carbonmonoxymyoglobin, from simulations and real data. The instrumental aspects of the experiment (highly intense X-ray beam, fast shutter system, Laue camera, detector, laser apparatus and synchronization technique) are emphasized.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 30 (1997), S. 153-163 
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The potential of very rapid Laue data collection for time-resolved studies down to the 150 ps timescale has been demonstrated in the case of cutinase, a 22 kDa lipolytic enzyme for which a considerable amount of structural information is available. This paper reports the derivation of the structure of native cutinase at 1.5 Å from a Laue data set recorded at the White Beam Station of the European Synchrotron Radiation Facility (ESRF), with a total exposure time of 8.5 ns. The structure of the heteromorphous mutant R196E was chosen as a starting model for refinement, in order to check whether these fast Laue data were of sufficient quality to allow an accurate structure determination from a strongly biased starting model. This analysis is relevant because similar situations are encountered in fast time-resolved experiments where rapid structural modifications of a protein are analysed from fast Laue data sets, recorded in some excited states of the protein, and from a structural model representative of the rest state. 19 Laue images were recorded with 150 ps X-ray pulses emitted by a single electron bucket from the ESRF storage ring. With two insertion devices used in series, tile available photon flux was sufficient to refine a satisfactory model of native cutinase (Rcryst = 19.3%; Rfree = 24.2%). Discrepancies between this model and an accurate atomic model of cutinase (obtained from monochromatic data collected to 1.0 Å, resolution, Rcryst = 9.7%) were minor and mainly due to the nonoptimal completeness of the data (71.7% to 1.5 Å) and to the different extent in resolution. The wild-type Arg196 could be readily positioned in the electron density and significant main- and side-chain displacements due to packing constraints were successfully retrieved with the Laue data. The electron-density maps were of sufficient quality to solve unambiguously these structural modifications. This feasibility study shows that very rapid Laue diffraction is a powerful tool to study protein dynamics in real time, provided that suitable macromolecular crystals as well as efficient reaction-triggering techniques are available.
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  • 10
    Electronic Resource
    Electronic Resource
    Chester : International Union of Crystallography (IUCr)
    Journal of synchrotron radiation 5 (1998), S. 215-221 
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The ESRF undulator beamline ID14 `Quadriga' is dedicated to monochromatic macromolecular crystallography. Using two undulators with 23 mm and 42 mm periods and a minimum gap of 16 mm installed on a high-β section, it will provide high-brilliance X-ray beams at around 13.5 keV, as well as a wide tuneability between 6.8 and 40 keV. Based on the Troika concept, this beamline has four simultaneously operating experimental stations: three side stations, EH1, EH2 and EH3, using thin diamond crystals, and an end station, EH4, with a fast-scan double-crystal monochromator. Station EH3 has a κ-diffractometer, and an off-line Weissenberg camera with a large 80 × 80 cm active area combined with a 2048 × 2048 CCD detector. During data collection the image plates are placed and removed by a robot located inside the hutch using a cassette system. After data collection the image plates are scanned with an off-line drum scanner. Station EH4 is designed for MAD applications, including Xe K-edge anomalous experiments, and is equipped with a 2048 × 2048 CCD detector on a pseudo 2θ arm. A common graphical user interface and a database will be available to cover all aspects of data collection, including strategy optimization. First results on the performance of the optics elements and initial crystallographic results are presented.
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