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31 citations found for Acharya, R.

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Neutron scattering has been employed to study the pore structure of a chromia-alumina catalyst. The results indicated the existence of three distinct scattering regimes with distinct slopes corresponding to the values of the wavevector, Q. The analysis of the scattering in these regions suggested that the large-Q region corresponds to Porod's law scattering and provides information on the specific surface area. The intermediate Q region arises from scattering from hollow capillaries and provides information on the dimension of the capillaries. The small-Q behaviour arises from the relative spatial arrangement of capillaries, which appear to form a `fractal' network.

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Acta Cryst. (1984). A40, C288
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The crystal structure of Cwp84, an S-layer protein from Clostridium difficile is presented for the first time. The cathepsin L-like fold of cysteine protease domain, a newly observed `lectin-like' domain and several other features are described.

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Two structures of Cwp84, a cysteine protease from the S-layer of C. difficile, are presented after propeptide cleavage. They reveal the movement of three loops, two in the active-site groove and one on the surface of the lectin-like domain, exposing a hydrophobic pocket.

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The detection and analysis of diffraction data from twinned macromolecular crystals is discussed, as is the recovery of useful data from these crystals.


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The structure of a tetragonal crystal form of C. botulinum C3 exoenzyme has been determined. NAD-induced main-chain flexure is concentrated in two lobes peripheral to a rigid [beta]-stranded core.

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The structure of foot-and-mouth disease virus (FMDV) strain O1 BFS 1860 has been determined to 2.9 Å resolution using the molecular-replacement method [Acharya, Fry, Stuart, Fox, Rowlands & Brown (1989). Nature (London), 337, 709-716]. Crystals of the virus with average dimensions 0.12 × 0.06 × 0.12 mm belong to space group I23, a = 345 Å with 1/12 of the icosahedral particle per asymmetric unit giving fivefold noncrystallographic redundancy. Oscillation diffraction photographs were collected at the SERC Synchrotron Radiation Source at Daresbury in accordance with strict disease security regulations. The ambiguity in particle orientation was resolved using a self-rotation function and starting estimates of the phases to 8 Å were derived from the known structures of two picornaviruses similarly oriented in the I23 unit cell. The phases were refined and extended using iterative averaging and solvent flattening with the implementation of a simple automatic envelope-determination procedure to increase the phasing power available.

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The human histone deacetylase sirtuin 1 was expressed and purified. Crystals were obtained and diffracted to 3.45 Å in space group P622.

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Acta Cryst. (2002). A58, c277
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