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Journal logoJOURNAL OF
ISSN: 1600-5775

January 2011 issue

3rd International Symposium on Diffraction Structural Biology (ISDSB2010)

Paris-Sud/XI University, Orsay, France, 25-28th May 2010

Highlighted illustration

Cover illustration: Images from presentations given at ISDSB2010. Centre: 70S ribosome crystal structure (courtesy of V. Ramakrishnan). Top right: neutron crystallography nuclear density maps of a singly protonated (left) and doubly protonated (right) histidine in haemoglobin (courtesy of Y. Morimoto). Bottom right: X-ray tomography reconstruction of the yeast S. pombe (courtesy of C. Larabell). Left: small-angle X-ray scattering rigid-body fitting for [alpha]-crustacyanin (from Rhys et al., pages 79-83).

facility information

diffraction structural biology

J. Synchrotron Rad. (2011). 18, 1
doi: 10.1107/S0909049510044912
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An introductory overview to the special issue papers on diffraction structural biology in this issue of the journal.

J. Synchrotron Rad. (2011). 18, 2-5
doi: 10.1107/S0909049510036812
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Based on the molecular architecture revealed by electron cryo-tomography, the mechanism of the bending motion of eukaryotic flagella/cilia is discussed.

J. Synchrotron Rad. (2011). 18, 6-10
doi: 10.1107/S0909049510028669
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The crystal structure of CutA1 from the psychrotrophic bacterium Shewanella sp. SIB1 in a trimeric form was determined at 2.7 Å resolution. This is the first crystal structure of a psychrotrophic CutA1.

J. Synchrotron Rad. (2011). 18, 11-15
doi: 10.1107/S0909049510028670
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A low-cost light-emitting diode (LED) UV source has been developed for facilitating macromolecular sample centring in the X-ray beam.

J. Synchrotron Rad. (2011). 18, 16-19
doi: 10.1107/S090904951003445X
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Three crystallization methods, including crystallization in the presence of a semi-solid agarose gel, top-seeded solution growth (TSSG) and a large-scale hanging-drop method, have previously been presented. In this study, crystallization has been further evaluated in the presence of a semi-solid agarose gel by crystallizing additional proteins. A novel crystallization method combining TSSG and the large-scale hanging-drop method has also been developed.

J. Synchrotron Rad. (2011). 18, 20-23
doi: 10.1107/S0909049510032449
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Crystal structures of a membrane protein transporter in three different conformational states provide insights into the transport mechanism.

J. Synchrotron Rad. (2011). 18, 24-28
doi: 10.1107/S090904951002772X
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Diffraction data to 3.2 Å from crystals of the 3.6 MDa erythrocruorin from a Brazilian earthworm represent the highest resolution reported to date for similar complexes. An unambiguous molecular replacement solution shows the particle to belong to the type I class.

J. Synchrotron Rad. (2011). 18, 29-30
doi: 10.1107/S0909049510030700
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Structural properties of plant nuclease TBN1 are studied using synchrotron radiation to explain its specificity, role of glycosylation and to contribute to potential application in cancer treatment.

J. Synchrotron Rad. (2011). 18, 31-36
doi: 10.1107/S0909049510041695
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Macromolecular crystallography at high pressure (HPMX) is a mature technique. Shorter X-ray wavelengths increase data collection efficiency on cryocooled crystals. Extending applications and exploiting spin-off of HPMX will require dedicated synchrotron radiation beamlines based on a new paradigm.

J. Synchrotron Rad. (2011). 18, 37-40
doi: 10.1107/S0909049510033601
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The collection of absorption and Raman spectroscopic data correlated with X-ray diffraction data allows investigators to understand the atomic structure as well as the electronic and vibrational characteristics of their samples, to identify transiently formed intermediates and to explore mechanistic questions. Raman spectroscopy instrumentation at beamline X26-C at the NSLS is currently available to the general user population.

J. Synchrotron Rad. (2011). 18, 41-44
doi: 10.1107/S0909049510036022
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A new beamline for simultaneous SAXS/WAXS of biomolecules in solution is described.

J. Synchrotron Rad. (2011). 18, 45-49
doi: 10.1107/S0909049510036009
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DING proteins constitute a recently discovered protein family that is ubiquitous in eukaryotes. The structural insights and the physiological involvements of these intriguing proteins are hereby deciphered.

J. Synchrotron Rad. (2011). 18, 50-52
doi: 10.1107/S0909049510032450
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The crystallization process can be controlled by protein surface shielding agents blocking undesirable competitive adhesion modes during non-equilibrium processes of deposition of protein molecules on the surface of growing crystalline blocks. The hypothesis is based on a number of experimental proofs from diffraction experiments and also retrieved from the Protein Data Bank.

J. Synchrotron Rad. (2011). 18, 53-57
doi: 10.1107/S0909049510029948
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In order to minimize the size of the X-ray source for a U-shaped rotating anticathode X-ray generator, the electron beam is focused over a short distance by a combined-function bending magnet. Simulation predicts that the beam brightness will reach almost 500 kW mm−2 for a 120 keV/75 mA beam.

J. Synchrotron Rad. (2011). 18, 58-61
doi: 10.1107/S0909049510034989
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Consecutive temporal analyses of enzyme structure have been performed during reactions in order to clarify the structure-based reaction mechanism. Four intermediate structures have been determined.

J. Synchrotron Rad. (2011). 18, 62-65
doi: 10.1107/S0909049510027718
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A binary complex between a low-molecular-weight purine nucleoside phosphorylase and ribose-1-phosphate is described for the first time and comparisons with known ternary complexes are drawn.

J. Synchrotron Rad. (2011). 18, 66-69
doi: 10.1107/S0909049510033595
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The structures of old yellow enzyme from Trypanosoma cruzi which produces prostaglandin F from PGH2 have been determined in the presence or absence of menadione.

J. Synchrotron Rad. (2011). 18, 70-73
doi: 10.1107/S0909049510036010
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Three research initiatives pursued by the Macromolecular Diffraction Facility at the Cornell High Energy Synchrotron Source (MacCHESS) are presented.

J. Synchrotron Rad. (2011). 18, 74-78
doi: 10.1107/S0909049510036824
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A lanthanoid complex, [Eu(DPA)3]3−, was used to obtain experimental phases at 4.0 Å resolution of PhTET1-12s, a large self-compartmentalized homo-dodecameric protease complex of 444 kDa.

J. Synchrotron Rad. (2011). 18, 79-83
doi: 10.1107/S0909049510034977
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The structure of α-crustacyanin has been determined to 30 Å resolution using negative-stain electron microscopy (EM) single-particle averaging and modelling with the β-crustacyanin dimer from the crystal structure (Protein Data Bank code 1gka), guided by PISA protein subunit interface calculations for 1gka, and compared with the protein arrangements observed in the crystal lattice of 1gka. This α-crustacyanin EM model has been checked against SAXS experimental data, including comparison with rigid-body models calculated from the SAXS data, and finally with analytical ultracentrifugation measurements.

J. Synchrotron Rad. (2011). 18, 84-87
doi: 10.1107/S0909049510035995
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Optimal salt concentration in a PEG-based crystallization solution is important for successful crystal growth and can be predicted prior to performing crystallization experiments.

J. Synchrotron Rad. (2011). 18, 88-91
doi: 10.1107/S0909049510037076

current events

J. Synchrotron Rad. (2011). 18, 92-93
doi: 10.1107/S0909049510051599

international union of crystallography

J. Synchrotron Rad. (2011). 18, 94-98
doi: 10.1107/S090904951004728X
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