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Cover illustration: A sulfanilic acid molecule creates a lattice interface in a crystal of porcine trypsin (p. 310). |
Acta Cryst. (2007). D63, 275 [ doi:10.1107/S0907444907005185 ] NumerologyZ. Dauter and E. N. BakerOnline 21 February 2007 |
Acta Cryst. (2007). D63, 276-281 [ doi:10.1107/S0907444906048499 ] Structure of the human p53 core domain in the absence of DNAY. Wang, A. Rosengarth and H. LueckeSynopsis: The crystal structure of the human p53 core domain in the absence of DNA has been determined with a new monoclinic space group (P21). Detailed analysis of non-crystallographic symmetry and crystal packing reveals that the p53 molecules are arranged differently from those in other p53 crystals, suggesting the possible existence of different p53 core domain tetramers. PDB reference: 2ocj Online 21 February 2007 |
Acta Cryst. (2007). D63, 282-287 [ doi:10.1107/S0907444906051638 ] Structure-based hypothesis on the activation of the CO-sensing transcription factor CooAM. Borjigin, H. Li, N. D. Lanz, R. L. Kerby, G. P. Roberts and T. L. PoulosSynopsis: The structure of a CooA variant from the thermophilic bacterium Carboxydothermus hydrogenoformans (ChCooA) is reported in which one monomer is fully in the on-state. PDB reference: 2hkx Online 21 February 2007 |
Acta Cryst. (2007). D63, 288-294 [ doi:10.1107/S0907444906051675 ] Structure of glutaredoxin Grx1p C30S mutant from yeastK. O. Håkansson and J. R. WintherSynopsis: The structures of S. cerevisae glutaredoxin 1 and of a fusion protein consisting of yellow fluorescent protein and glutaredoxin were solved by molecular replacement and refined to 2.0 and 2.7 Å, respectively. Online 21 February 2007 |
Acta Cryst. (2007). D63, 295-301 [ doi:10.1107/S0907444906052024 ] His-tag impact on structureM. Carson, D. H. Johnson, H. McDonald, C. Brouillette and L. J. DeLucasSynopsis: Crystal structures with and without His-tags have been surveyed and the authors show that His-tags are not hazardous to your structure. Online 21 February 2007 |
Acta Cryst. (2007). D63, 302-309 [ doi:10.1107/S0907444906053261 ] Reduction of X-ray-induced radiation damage of macromolecular crystals by data collection at 15 K: a systematic studyA. Meents, A. Wagner, R. Schneider, C. Pradervand, E. Pohl and C. Schulze-BrieseSynopsis: A small but significant reduction of X-ray-induced radiation damage at 15 K compared with 90 K could be found in the systematic study of a total of 54 crystals of insulin and holoferritin. Online 21 February 2007 |
Acta Cryst. (2007). D63, 310-318 [ doi:10.1107/S0907444906053303 ] A novel strategy for the crystallization of proteins: X-ray diffraction validationS. B. Larson, J. S. Day, R. Cudney and A. McPhersonSynopsis: Difference Fourier X-ray diffraction analyses of nine crystals are presented, which convincingly demonstrate the validity of the hypothesis that protein crystallization can be driven by the inclusion of small molecules rich in hydrogen-bonding, hydrophobic and electrostatic bonding possibilities. Online 21 February 2007 |
Acta Cryst. (2007). D63, 319-327 [ doi:10.1107/S0907444906053649 ] Nonstoichiometric complex of gramicidin D with KI at 0.80 Å resolutionA. Olczak, M. L. Glówka, M. Szczesio, J. Bojarska, W. L. Duax, B. M. Burkhart and Z. WawrzakSynopsis: Structure of double-stranded right-handed double-helical gramicidin channels (dimers) in the crystal of gramicidin D with KI complex has been determined. High-resolution data enabled quantitative determination of gramicidin components and distributions of the I anions outside and K cations inside the channel, which was confirmed by their anomalous scattering. PDB reference: 2izq Online 21 February 2007 |
Acta Cryst. (2007). D63, 328-338 [ doi:10.1107/S0907444906053625 ] Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agentsS. P. Muench, S. T. Prigge, R. McLeod, J. B. Rafferty, M. J. Kirisits, C. W. Roberts, E. J. Mui and D. W. RiceSynopsis: The crystal structures of T. gondii and P. falciparum ENR in complex with NAD+ and triclosan and of T. gondii ENR in an apo form have been solved to 2.6, 2.2 and 2.8 Å, respectively. PDB references: 2o2y, 2o2s and 2o50 Online 21 February 2007 |
Acta Cryst. (2007). D63, 339-347 [ doi:10.1107/S0907444906054230 ] A methodology and an instrument for the temperature-controlled optimization of crystal growthM. Budayova-Spano, F. Dauvergne, M. Audiffren, T. Bactivelane and S. CusackSynopsis: A methodology and an instrument for the temperature-controlled optimization of crystal growth are described. The technique finds application in the growth of large high-quality crystals for neutron crystallography. Online 21 February 2007 |
Acta Cryst. (2007). D63, 348-354 [ doi:10.1107/S0907444906055065 ] An extremely SAD case: structure of a putative redox-enzyme maturation protein from Archaeoglobus fulgidus at 3.4 Å resolutionO. Kirillova, M. Chruszcz, I. A. Shumilin, T. Skarina, E. Gorodichtchenskaia, M. Cymborowski, A. Savchenko, A. Edwards and W. MinorSynopsis: The SAD technique was used to determine the crystal structure of a putative redox-enzyme maturation protein from A. fulgidus at 3.4 Å resolution. PDB reference: 2o9x Online 21 February 2007 |
Acta Cryst. (2007). D63, 357-365 [ doi:10.1107/S0907444906055442 ] Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphateS. Yoshikawa, R. Arai, Y. Kinoshita, T. Uchikubo-Kamo, T. Wakamatsu, R. Akasaka, R. Masui, T. Terada, S. Kuramitsu, M. Shirouzu and S. YokoyamaSynopsis: The crystal structure of glyoxylate reductase from the hyperthermophilic archaeon P. horikoshii OT3 complexed with NADP(H) was solved at 1.7 Å resolution. The present study revealed its cofactor-recognition and thermostability mechanisms. PDB references: 2dbq, 2dbz and 2dbr Online 21 February 2007 |
Acta Cryst. (2007). D63, 366-380 [ doi:10.1107/S0907444906055624 ] On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengthsC. Mueller-Dieckmann, S. Panjikar, A. Schmidt, S. Mueller, J. Kuper, A. Geerlof, M. Wilmanns, R. K. Singh, P. A. Tucker and M. S. WeissSynopsis: The anomalously scattering substructures in 23 crystals of 19 different biological macromolecules have been determined based on diffraction data collected at a wavelength of 2.0 Å. PDB references: 2g4h, 2g4i, 2g4j, 2g4k, 2g4p, 2g4q, 2g4l, 2g4m, 2g4n, 2g4o, 2g4p, 2g4s, 2g4t, 2g4u, 2g4v, 2g4w, 2g4x, 2g4y, 2g4z, 2ill, 2g51, 2g52 and 2g55 Online 21 February 2007 |
Acta Cryst. (2007). D63, 381-389 [ doi:10.1107/S0907444906056204 ] Structural asymmetry and intersubunit communication in muscle creatine kinaseJ. F. Ohren, M. L. Kundracik, C. L. Borders, P. Edmiston and R. E. ViolaSynopsis: The structure of a transition-state analog of muscle creatine kinase reveals significant asymmetry within the functional homodimer. The amino-terminal region is shown to be intimately involved in subunit association and intersubunit communication. PDB reference: 1u6r Online 21 February 2007 |
Acta Cryst. (2007). D63, 390-400 [ doi:10.1107/S090744490605640X ] Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshiiR. Fukunaga and S. YokoyamaSynopsis: The crystal structure of the AlaX-M trans-editing enzyme revealed that the conserved glycine-rich loop in the N-terminal domain is located near the catalytic site in the C-terminal domain. PDB reference: 2e1b Online 21 February 2007 |
Acta Cryst. (2007). D63, 401-407 [ doi:10.1107/S0907444906056435 ] Double-stranded helical twisted
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Acta Cryst. (2007). D63, 408-414 [ doi:10.1107/S0907444907000182 ] Structures of two mutants that probe the role in iron release of the dilysine pair in the N-lobe of human transferrinH. M. Baker, D. Nurizzo, A. B. Mason and E. N. BakerSynopsis: The crystal structures of two mutants of the N-terminal half-molecule of human transferrin, K206E and K206E/K296E, have identified important features of the mechanism of iron release. Online 21 February 2007 |
Acta Cryst. (2007). D63, 415-419 [ doi:10.1107/S090744490605270X ] Slow diffusion of lactose out of galectin-3 crystals monitored by X-ray crystallography: possible implications for ligand-exchange protocolsP. M. Collins, K. I. P. J. Hidari and H. BlanchardSynopsis: Structures of human galectin-3 carbohydrate-recognition domain determined at various stages of ligand removal provided insight into ligand-diffusion rates and their significance with respect to ligand-exchange protocols. PDB references: 2nn8, 2nmo and 2nmn Online 21 February 2007 |
Acta Cryst. (2007). D63, 420 [ doi:10.1107/S0907444906056113 ] PET Chemistry. The Driving Force in Molecular ImagingOnline 21 February 2007 |
Acta Cryst. (2007). D63, 421-423 [ doi:10.1107/S0907444907006336 ] Deposition of structural data reduxA. WlodawerOnline 21 February 2007 |
Acta Cryst. (2007). D63, 424-429 [ doi:10.1107/S0907444907007846 ] Notes for authors 2007Online 21 February 2007 |
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