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Notes: Crystal structure solution by anomalous dispersion methods has been greatly facilitated using the rapidly tunable station 9.5 at the Daresbury SRS. Both SIROAS and MAD techniques, with IP data, have been used in the phasing of a brominated nucleotide and a seleno deaminase, respectively. The electron density maps in each case are interpretable. Throughput of projects could be improved upon with a better duty cycle detector. Another category of data collection is that at very high resolution. Detailed structure refinement pushes the limits of resolution and data quality. Station 9.5 has been used to collect high resolution (1.4 A(ring)) native data for the protein concanavalin A. This utilized very short wavelengths (0.7 A(ring)), the image plate, and crystal freezing. A total of 155 407 measurements from two crystals benefited from the on-line nature of the IP detector device, but a slow and quick pass are required to capture the full dynamic range of the data. There are data seen to 1.2 A(ring) and beyond for a pure Mn substituted form of the protein, but a higher intensity still is required to actually record these data. By comparison, trials at CHESS, on a multipole wiggler (station A1) with a CCD (without image intensifier) system, yield native concanavalin A data to 0.98 A(ring) and beyond. This demonstrates that the combination of yet higher intensity and the ease of use of a CCD offers worthwhile improvements; in this case an increase in the data by a factor of (1.4/0.98)3, thus at least doubling the data to parameter ratio for protein structure model refinement and potentially opening up direct structure determination of proteins of the size of concanavalin A (25 kDa).Finally, possibilities at ESRF and further detector developments, such as mosaic CCDs and scintillator coatings, offer further impetus for the field. These include more intense rapidly tunable beams for anomalous dispersion-based structure solution and "ideal'' higher resolution data collection and reactivity studies. ESRF BL19 is described; facilities on BL19 will include a system for freezing and storing crystals at cryogenic temperatures, so that data can be recorded from the same crystal on different runs. Overall, there have been tremendous strides made in this field in the last 15 years, and yet further improvements are to come. © 1995 American Institute of Physics.

Notes: Single-crystal x-ray diffraction data can be measured very quickly in Laue geometry compared with monochromatic methods. Alternatively, this gain factor can be used instead to reduce the sample volume for a fixed exposure time. In the latter case especially, there is a critical need to control parasitic scatter in the Laue camera. The use of Laue geometry as a means of quantitative data acquisition required the solution of some fundamental problems. The so-called "overlapping orders problem'' has been found not to be limiting. It can be shown that the bulk of the Laue spots are single order, provided dhkl〈2dmin where dhkl is the interplanar spacing and dmin is the resolution limit of the data. In addition, empirical wavelength normalization is required. This can be achieved by using the symmetry of the diffraction pattern. The fact that different equivalents occur at different wavelengths means that the differences in these intensities can be used to establish the "λ curve.'' Successful wavelength normalization to date has used a relatively broad-band pass. The multiplicity distribution is the histogram of the number of spots of a given order. This distribution is determined by the ratio λmax/λmin (λmax =maximum wavelength, λmin =minimum wavelength in the beam). λmax is determined by the use of any filters in the beamline. λmin is determined either by the spectral curve or a critical cutoff if a mirror is used. A mirror can be usefully introduced to enhance the multiplicity distribution in favor of single wavelength spots or to focus the white beam; so far only vertical focussing has been used. The detector options used to date have been photographic film, Fuji image plate (at Photon Factory)/Kodak storage phosphor (at Cornell) and charge coupled device (CCD) (at Daresbury). It is useful to consider the joint theoretical spatial and energy distribution of spots in defining the detector specification and geometry. To date, we have processed Laue film data successfully. The attraction of using the CCD, even to look at a small portion of the Laue pattern, is to view the diffraction in real time.This will allow tight control of parasitic scatter for microcrystal Laue diffraction and real-time monitoring for time-resolved work. We performed initial experiments using a direct detection CCD imager, and have obtained satisfactory diffraction data on a 40 ms time scale. Results of this work will be presented. In order to assess the efficacy of the Laue method for quantitative crystallography, we have used Laue data from the protein pea lectin and compared it in detail with monochromatic pea lectin data. To assess the use of a vertically focussing mirror, we have successfully used a mercury derivative protein crystal to yield isomorphous and anomalous differences suitable for phase determination. In both the pea lectin and mercury derivative cases, doublet Laue spots were deconvoluted. In the latter case, the data were used in a difference Fourier calculation which showed the mercury peak. Future developments and projections based on multipole sources are given.

Notes: There exists considerable promise for the use of charge-coupled device (CCD) imagers in the fast recording of parts of macromolecular crystal Laue diffraction patterns. As part of this development CCD tests have been made with direct detection of Laue patterns from a small molecule test crystal and a protein crystal. Merging R factors (on intensity), for strong reflections, of 3% have been obtained. A time-slicing scheme for a CCD camera is discussed based on the stacking of slices held in storage in the CCD in the submillisecond time resolution range.

Notes: Area X-ray detectors based on charge-coupled device imagers can provide excellent performance in terms of spatial resolution, sensitivity and dynamic range. Improvements in the fabrication of the primary converter, either scintillator or phosphor, mean that it is becoming possible to dispense with prestorage intensifiers and still provide outstanding low-level signal performance. Structured CsI scintillators are presented as one method of providing high efficiency and excellent spatial resolving power for this primary converter. Characterization of detector performance, in terms of such parameters as the detective quantum efficiency, point-spread function and dynamic range, needs to be directly related to the specific application of the detector. This contribution emphasizes the interplay of these parameters in the optimum design of detector systems. Performance prediction, based on measurements taken from prototype development systems, illustrates how such detectors will meet the exacting requirements of macromolecular crystallography.