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  • 1995-1999  (13)
  • 1985-1989  (4)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 7968-7973 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1089-7623
    Source: AIP Digital Archive
    Topics: Physics , Electrical Engineering, Measurement and Control Technology
    Notes: The existence of crystal glitches in EXAFS data is widely recognized and is usually dealt with during data analysis. However, in many cases, especially as samples become more dilute, the disruption of the data can become irretrievable. The advent of new, high output, double-crystal x-ray monochromators has made it necessary to investigate the cause of such glitches with a view to reducing them in the original data. The occurrence of multiple reflections within the crystal gives rise to the glitches seen in EXAFS data when the two crystals in a double-crystal monochromator are not accurately aligned. The results of a simple alignment of such a double-crystal monochromator are presented and show a reduction of the glitches in the recorded data. A purpose-built monochromator for further investigation of this problem is described and some results towards the further reduction of glitches are presented. It is shown that the removal of crystal glitches from EXAFS data is possible
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 111 (1989), S. 102-107 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 30 (1997), S. 770-775 
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The model-independent approach based on the multipole expansion method using spherical harmonics [Stuhrmann (1970a). Acta Cryst. A26, 297–306] has been applied to obtain structural information on a variety of metalloproteins studied by synchrotron X-ray solution scattering. The method is applied to examples (nitrite reductase, transferrin and nitrogenase), not only with the view of comparing protein conformations in solution with those in the crystalline state, but also defining conformational changes and protein-protein interactions which are of functional importance. The shape restoration is found to be straightforward at low resolution (L≤ 3). For correct treatment using higher harmonics, overall molecular symmetry, if present, must be included in the multipole expansion.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Chester : International Union of Crystallography (IUCr)
    Journal of synchrotron radiation 3 (1996), S. 14-19 
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: We have recently demonstrated that X-rays can be used for changing the redox states of the metal centre in metalloproteins [Murphy et al. (1995). J. Synchrotron Rad. 2, 64–69]. The possibility of using the Laue method for studying the structural changes associated with such X-ray-induced reactions is explored by applying the method to the structure determination of a new azurin (hereafter referred to as azurin II) from the denitrifying bacterium Alcaligenes xylosoxidans. Laue X-ray diffraction data of azurin II were collected at station 9.7 of the SRS Daresbury. Three diffraction patterns were recorded on film packs at three different crystal orientations. The data were processed using the Daresbury Laue Software Suite to give 2224 independent single reflections (Rmerge = 0.136) in the wavelength range 0.36–1.40 Å. The data completeness was 44% at 2.55 Å resolution. Phase determination for the data was undertaken using the molecular-replacement method; the top peak was chosen in both the rotation function and the subsequent translation function. This solution agreed well with the molecular-replacement solution achieved independently using monochromatic data. The electron-density map showed reasonably good agreement with the model and the copper site was readily recognizable as it had the highest density. To see if the electron-density map could be improved, `the doublets in the diffraction data were then deconvoluted. This added 26% data in the region ∞-2dmin resulting in an improvement in the data completeness to 50% and thus in improved continuity of the electron-density map. The quality of these maps is discussed from the point of view of the suitability of this approach for studying redox-induced structural changes.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The quick EXAFS (QuEXAFS) technique provides an alternative way of recording X-ray absorption fine-structure (XAFS) data where the scan time is reduced by moving the monochromator at a constant angular speed and recording the data `on the fly'. Results are presented to show that the use of fluorescence detection with QuEXAFS is eminently suitable for studying reactions in dilute systems such as metalloproteins at a sub-minute time scale. In addition, we show that the fluorescence–QuEXAFS technique can reduce the overall time for normal data collection by some 50% compared with conventional step-by-step scanning EXAFS using the same optical system, thus reducing the total X-ray exposures of the samples. The use of X-rays for studying in situ redox reactions is demonstrated.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Chester : International Union of Crystallography (IUCr)
    Journal of synchrotron radiation 3 (1996), S. 185-196 
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Fitting an entire X-ray spectrum rather than its components, EXAFS and XANES, has been an aim of the practitioners of these techniques. Recent developments have made the calculations of both the scattering and atomic components practicable. We present the analysis of four representative model compounds using the EXCURVE package, which was modified to undertake this. The details of these modifications are also given. A comparison of matrix-inversion and finite-path-sum methods is made which shows that the latter method is more promising for fitting the edge region. A number of enhancements are required before this approach can be used for accurate structure determination. These include improvement in atomic contribution, better potentials/phase shifts, and the ability to calculate and refine multiple-scattering terms to at least fifth order.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 1052-1064 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: It has been reported previously that Alcaligenes xylosoxidans (NC1MB 11015) grown under denitrifying conditions produces two azurins instead of the single previously identified azurin [Dodd, Hasnain, Hunter, Abraham, Debenham, Kanzler, Eldridge, Eady, Ambler & Smith (1995). Biochemistry. In the press]. The new azurin, called azurin II, has been crystallized as blue elongated rectangular prisms with the tetragonal space group P4122 and unit-cell parameters a = b = 52.65, c = 100.63 Å. X-ray crystallographic data extending to 1.9 Å resolution were collected by the Weissenberg method using 200 × 400 mm image plates and synchrotron X-rays of wavelength 0.97 Å. The three-dimensional structure of azurin II has been solved by the molecular-replacement method using the structure of azurin from Alcaligenes denitrificans NCTC 8582 with which this new azurin shows a close homology. The quality of the initial map was sufficient to predict a number of sequence differences. The model is currently refined to an R-factor of 18.8% with X-ray data between 8.5 and 1.9 Å. The final model of 961 protein atoms, one Cu atom and 50 water molecules has r.m.s. deviations from ideality of 0.009 Å for bond lengths and 1.7° for bond angles. The overall structure is similar to that of the azurin from A. denitrificans NCTC 8582. It has a β-barrel structure with the Cu atom located near the top end of the molecule. The Cu atom is coordinated to Nδ of His46 and His117 at 2.02 Å and to Sγ of Cys112 at 2.12 Å, while the carbonyl O atom of Gly45 and Sδ atom of Met121 provide the additional interactions at 2.75 and 3.26 Å, respectively.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 243-246 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Solving the phase problem is the crucial and quite often the most difficult and time-consuming step in crystallographic structure determination. The traditional methods of isomorphous replacement (MIR or SIR) and molecular replacement require the availability of an isomorphous heavy-atom derivative or the structure of a homologous protein, respectively. Here, a method is presented which utilizes the low-resolution molecular shape determined from solution X-ray scattering data for the molecular search. The molecular shape of a protein is an important structural property and can be determined directly by the small-angle scattering technique. The idea of locating this molecular shape in the crystallographic unit cell has been tested with experimental diffraction data from nitrite reductase (NiR). The conventional Patterson search proved to be unsuccessful, as the intra-envelope vectors are uniformly distributed and do not match those of intra-molecular (atom-to-atom) vectors. A direct real-space search for orientation and translation was then performed. A self-rotation function using 2.8 Å crystallographic data yielded the polar angles of the non-crystallographic threefold axis. Knowledge of the orientation of this axis reduces the potential six-dimensional search to four (Eulerian angle γ and three translational parameters). The direct four-dimensional search within the unit cell produced a clear solution. The electron-density map based on this solution agrees well with the known structure, and the phase error calculated from the map was 61° within 20 Å resolution. It is anticipated that the low-resolution envelope can be used as a starting model for phase extension by the maximum-entropy and density-modification method.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The structure of rusticyanin is the largest unknown structure (Mr = 16.8 kDa) which has been recently solved by the direct-methods approach using only single-wavelength anomalous scattering (SAS) data from the native protein [Harvey et al. (1998). Acta Cryst. D54, 629–635]. Here, the results of the Sim distribution approach [Hendrickson & Teeter (1981). Nature (London), 290, 107–113] and of the CCP4 procedure MLPHARE [Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760–763] are compared with those from direct methods. Analysis against the final refined model shows that direct methods produced significantly better phases (average phase error 56°) and therefore significantly better electron-density maps than the Sim distribution and MLPHARE approaches (average phase error was around 63° in both cases).
    Type of Medium: Electronic Resource
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