issue contents

ISSN: 2052-2525

March 2014 issue

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Biological crystallography has never been more vibrant. Celebrating this, IUCrJ invites high-impact papers from across the whole spectrum of structural biology and medicine.

scientific commentaries

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A brief history is given of how X-ray diffraction data from crystals have been recorded. Today there are new possibilities, spawned by the availability of free electron lasers that produce powerful femtosecond long X-ray pulses.

research papers

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The structure solution of T. brucei cathepsin B from 80 in vivo grown crystals with an average volume of 9 µm3 obtained by serial synchrotron crystallography at a microfocus beamline is reported.

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The plant purple acid phosphatase PPD1 forms a novel hexameric structure with a fibronectin III-like domain that is involved in DNA selectivity, binding and activation. The degradation of DNA by PPD1 implies a role for PPD1 in plant growth and repair and in pathogen defence.

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Multi-temperature single-crystal and powder diffraction experiments on 1-(2′-aminophenyl)-2-methyl-4-nitroimidazole show that this crystal undergoes an isomorphic phase transition with the coexistence of two phase domains over a wide temperature range. The anharmonic approach was the only way to model the resulting disorder.

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An enrichment ratio is derived from the decomposition of the crystal contact surface between pairs of interacting chemical species. The propensity of different contact types to form is investigated.

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Human carbonic anhydrases are zinc metalloenzymes that catalyze the hydration and dehydration of CO2 and HCO3, respectively. X-ray crystal structures of a variant of human carbonic anhydrase II in complex with four imidazole derivatives (imidazole, 1-methylimidazole, 2-methylimidazole and 4-methylimidazole) have been determined in order to identify the binding sites for such compounds, and a mechanism to explain the effects on catalytic activity is proposed.

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Multi-component crystals of the anti-inflammatory drug acemetacin were prepared by melt crystallization and their X-ray crystal structures solved using single-crystal and high-resolution powder X-ray diffraction (PXRD) data. The acemetacin–para-aminobenzoic acid adduct and the acemetacin piperazine salt are stable to hydration in the aqueous medium (up to 24 h).
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