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108 citations found for Hasnain,

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Acta Cryst. (1987). A43, C29
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The CRP/FNR family transcription factor from M. tuberculosis H37Rv has been crystallized in space group P212121 in the absence of cAMP. The crystals show the presence of a dimeric molecule in the asymmetric unit.

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Structures of inhibitor-bound bovine cytochrome bc1 were determined by cryo-EM and compared with X-ray crystallographic structures, demonstrating that cryo-EM could be a feasible tool for structure-based drug discovery.


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The structure of D-lactate dehydrogenase from Aquifex aeolicus has been determined with each subunit of the homodimer in a `closed' conformation and with the NAD+ cofactor and lactate (or pyruvate) bound at the inter-domain active-site cleft.

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The structure of the stationary phase survival protein SurE protein from the hyperthermophile Aquifex aeolicus has been solved to 1.5 Å resolution. The divalent-metal-ion-dependent phosphatase active-site pocket is occupied by sulfate ions from the crystallization medium.

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The structure of a glyceraldehye 3-phosphate dehydrogenase from a denitrifying bacterium has been determined at 1.7 Å resolution. It confirms the essential role of Cys154 in the enzyme's activity.

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The structure of a protein involved in the molybdopterin and molybdenum co-factor biosynthesis pathways of Sulfolobus tokodaii has been solved to a resolution of 1.9 Å.


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An overview of the second special issue of the journal on biological applications of X-ray absorption spectroscopy is presented.

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Acta Cryst. (2002). A58, c117
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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.

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Neutron crystallography and sub-atomic X-ray crystallography complement each other in defining hydrogen positions in macromolecules. Significant advances have been made but much effort is still required if neutron crystallography is to become a mainstream activity.

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Insight is provided into the dynamic interactions of LAT1 and CD98hc and their role in the transport cycle of the complex.

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A new MAD beamline at the SRS (UK) for structural genomics and proteomics has been recently commissioned. The beamline is based on a 20 mm external gap, 2.46 T ten-pole wiggler with highly optimized optics to provide rapid (subsecond) tunability over an edge and the highest intensity radiation over 5 to 13.5 keV. An energy-dispersive high-count-rate fluorescence detector with large active area is also integrated into the crystallographic set-up providing unique capabilities to this MAD station.

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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 [infinity]-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.

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