This page contains a selection of articles from Crystallography Journals Online that have been highlighted in the IUCr newsletter.
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  Acta Cryst. (2008). A64, 359-367 [ doi:10.1107/S0108767308004807 ] An investigation into structural changes due to deuterationS. J. Fisher and J. R. HelliwellThere has been a growth in the experimental determination of the protonation states of proteins. In this study the effect of deuteration on structure was examined by data mining, which yielded 52 small-molecule crystal structures as deuterated and hydrogenated pairs. Differences between these small-molecule structures have been calculated and the results thus far follow the initial assumption. With time, it will become possible to analyse for any differences, at a significant level of precision, of a large cohort of ultra-high-resolution protein structures in H and D forms. |  Superimposed bis(3-amino-3-methyl-2-butanone oximato)nickel(II) chloride monohydrate (AMBONC) structures. Deuterated structure shown in blue and hydrogenated in green. | |
        Acta Cryst. (2008). B64, 240-248 [ doi:10.1107/S0108768108004813 ] Structures of mono-unsaturated triacylglycerols. III. The |  Rietveld refinement result of  1′-2 PEP (1,3-dipalmitoyl-2-elaidoylglycerol) from high-resolution laboratory data and packing view parallel to the b axis. | |
      Acta Cryst. (2008). C64, m205-m208 [ doi:10.1107/S010827010800824X ] Two scandium-biuret complexes: [Sc(C2H5N3O2)(H2O)5]Cl3·H2O and [Sc(C2H5N3O2)4](NO3)3W. T. A. HarrisonFormula: [Sc(C2H5N3O2)(H2O)5]Cl3·H2O and [Sc(C2H5N3O2)4](NO3)3 Scandium(III) shows unusual flexibility in its coordination number in complexes, and six-, seven-, eight- and nine-coordinate species are known. When combined with biuret and water molecules, distinctive, near regular, pentagonal bipyramidal [Sc(H2O)5(C3H5N2)]3+ and square antiprismatic [Sc(C3H5N2)4]3+ geometries arise, suggesting that the counter-ion may play some role in defining the metal coordination preference. |  The molecular structure of [Sc(C3H5N2)4]3+. | |
  Acta Cryst. (2008). D64, 567-588 [ doi:10.1107/S0907444908006082 ] Charge-density analysis of a protein structure at subatomic resolution: the human aldose reductase caseB. Guillot, C. Jelsch, A. Podjarny and C. LecomteX-ray synchrotron diffraction data are available for human aldose reductase up to 0.66 Å resolution. The protein electron density was refined using a multipolar atom model. Chemically equivalent atoms were constrained to have the same electron density. The refined electron density agrees well with our experimental multipolar atoms database, especially for atoms with many copies in the protein. Upon database transfer, atomic thermal parameters showed a small but systematic decrease. According to the main-chain bond lengths, stereochemical dictionaries may be revised. |  Deformation of the protein electron density in the peptide bond plane. The blue colour accounts for the accumulation of electron density on the covalent bonds and lone pairs. | |
        Acta Cryst. (2008). E64, o841 [ doi:10.1107/S1600536808009677 ] 8-Methyl-5-methylene-2-oxotricyclo[5.3.1.13,9]dodecan-endo-8-olI. Y. H. Chan, R. Bishop, D. C. Craig, M. L. Scudder and W. YueThe racemic molecules of this tricyclic compound undergo a considerable degree of enantiomer separation during crystallization. They assemble by means of O–H...O=C hydrogen-bonded interactions into parallel enantiomerically pure chains oriented along the b direction, and then further aggregation of these chains results in formation of homochiral layers in the ab plane. This type of crystallization outcome, midway between intimate mixing of the enantiomers and conglomerate formation, is a poorly understood phenomenon. |  Unit-cell diagram showing the O–H...O=C hydrogen-bonded chain along b. Adjacent layers along c are chirally pure with alternating chirality. This is indicated by light- and dark-green shading of C atoms. | |
  Acta Cryst. (2008). F64, 156-162 [ doi:10.1107/S1744309108001413 ] Structure of mouse ADP-ribosylhydrolase 3 (mARH3)C. Mueller-Dieckmann, S. Kernstock, J. Mueller-Dieckmann, M. S. Weiss and F. Koch-NolteADP-ribosylation is a reversible posttranslational modification that modulates protein activity in pro- and eukaryotes. The reaction is catalysed by ADP-ribosyltransferases (ARTs) and ADP-ribosylhydrolases (ARHs), respectively. ARTs and ARHs have been divided into a number of subfamilies that are thought to confer substrate specificity. The structure of mouse ADP-ribosylhydrolase 3 has been solved to a resolution of 1.8 Å and is featured as an interactive figure in this publication. Two Mg ions are located in a cleft on the protein surface that pinpoint the active site. |  | |
  J. Appl. Cryst. (2008). 41, 237-248 [ doi:10.1107/S0021889808000617 ] Evaluation of the focusing performance of bent Laue crystals using wave-optical theoryY. I. Nesterets and S. W. WilkinsBent-Laue-crystal optics has proved to be one of the very few optical elements that allows one to focus wide beams of high-energy X-rays (above 30 keV) with high efficiency. The geometrical optics approximation, traditionally used for evaluating the performance of such crystals, has serious limitations on its validity. In our approach, quantitative analysis of the focusing performance of bent Laue crystals is carried out using numerical simulations of the process of propagation of spherical waves through the optical system, based on a rigorous wave-optics treatment, with some significant new findings. |  Intensity distribution at different distances from a cylindrically bent Laue crystal. | |
   J. Synchrotron Rad. (2008). 15, 123-128 [ doi:10.1107/S0909049507061468 ] Migration of mercury from dental amalgam through human teethH. H. Harris, S. Vogt, H. Eastgate, D. G. Legnini, B. Hornberger, Z. Cai, B. Lai and P. A. LayIngestion of mercury from dental amalgams, with possible negative health effects, has generally been considered to occur directly from filling surfaces. The importance of mercury exposure by direct migration through the tooth was examined by X-ray fluorescence imaging of Hg, Ca, Zn and Cu in human teeth filled with amalgam for more than twenty years. The detection of Hg in areas of the tooth that once contained an active bloodstream and in calculus indicates that both exposure pathways should be considered as significant. |  | |
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2-hydroxido-bis[dioxouranium(VI)]]-di-2-2-pyridylacetato-![[kappa]](/logos/entities/kappa_rmgif.gif)
3O,N:O';3O:O',N]. Acta Cryst. C64, m50-m52. 
3-1,1-dioxo-1,2-benzoisothiazole-3-thiolato-3N:S3:S3)silver(I)]. Acta Cryst. C63, m395-m397. 2S,S')bismuth(III). Acta Cryst. E62, m2552-m2554. 5-hydrogenphosphato-pentamolybdate(VI) tetrahydrate. Acta Cryst. C62, m355-m357. ![[alpha]](/logos/entities/alpha_rmgif.gif)
-GaPO4. Acta Cryst. A62, 1-10. -tetraethoxyborato]. Acta Cryst. C61, m417-m418. ![[eta]](/logos/entities/eta_rmgif.gif)
5-cyclopentadienyl)tungstenio]indium. Acta Cryst. E61, m945-m946. -acetato-acetonitriletris(-N,N'-diphenylformamidinato)diruthenium tetrafluoroborate dichloromethane hemisolvate. Acta Cryst. C61, m71-m73. -chloro-bis[dichloropalladium(II)]. Acta Cryst. C60, m426-m430.