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Cover illustration: A photomontage of crystal micrographs from papers published in Acta Cryst. F in 2007. Top row: putative zinc transporter CzrB from Thermus thermophilus (Höfer et al., pp. 673-677); tetrasulfocyanine, a fluorescent probe, in complex with the Fab antibody fragment MOR03268 (Hillig et al., pp. 217-223); and the homing endonuclease I-Dmo-I in complex with its target DNA (Redondo et al., pp. 1017-1020). Middle row: an Escherichia coli tRNAGly acceptor-stem microhelix (Förster et al., pp. 46-48); BigR, a transcription repressor from Xylella fastidiosa (Barbosa et al., pp. 596-598); and PH1010 from Pyrococcus horikoshii OT3 (Shirokane et al., pp. 532-534). Bottom row: the N-terminal region of the human formin-homology protein FHOD1 (Schulte et al., pp. 878-881); the archaeal transcription termination factor NusA (Tanaka et al., pp. 69-73); and Escherichia coli WrbA in complex with its cofactor flavin mononucleotide (Wolfová et al., pp. 571-575). |
Acta Cryst. (2008). F64, 1 [ doi:10.1107/S1744309107066456 ]
Online 20 December 2007
Acta Cryst. (2008). F64, 2-7 [ doi:10.1107/S1744309107065931 ] Structure of HsaD, a steroid-degrading hydrolase, from Mycobacterium tuberculosisN. Lack, E. D. Lowe, J. Liu, L. D. Eltis, M. E. M. Noble, E. Sim and I. M. WestwoodSynopsis: The structure of HsaD, a carbon-carbon bond serine hydrolase involved in steroid catabolism that is critical for the survival of M. tuberculosis inside human macrophages, has been solved by X-ray crystallography. Data were collected at the Diamond Light Source in Oxfordshire, England: this paper describes one of the first structures determined at the new synchrotron. PDB reference: 2vf2 Online 20 December 2007 |
Acta Cryst. (2008). F64, 8-13 [ doi:10.1107/S1744309107066481 ] The structure of melon necrotic spot virus determined at 2.8 Å resolutionY. Wada, H. Tanaka, E. Yamashita, C. Kubo, T. Ichiki-Uehara, E. Nakazono-Nagaoka, T. Omura and T. TsukiharaSynopsis: The structure of melon necrotic spot virus is reported. PDB reference: 2zah Online 20 December 2007 |
Acta Cryst. (2008). F64, 14-18 [ doi:10.1107/S1744309107057260 ] Semi-automated microseeding of nanolitre crystallization experimentsT. S. Walter, E. J. Mancini, J. Kadlec, S. C. Graham, R. Assenberg, J. Ren, S. Sainsbury, R. J. Owens, D. I. Stuart, J. M. Grimes and K. HarlosSynopsis: A procedure for microseeding into nanolitre crystallization drops is described with selected successful examples. Online 20 December 2007 |
Acta Cryst. (2008). F64, 19-21 [ doi:10.1107/S1744309107059696 ] Crystallization and preliminary X-ray studies of SdiA from Escherichia coliC. Wu, N. K. Lokanath, D. Y. Kim, L. D. N. Nguyen and K. K. KimSynopsis: E. coli SdiA was overexpressed, purified and crystallized. The crystals belonged to the hexagonal space group P6122 or P6522 and diffracted to 2.7 Å resolution. Online 20 December 2007 |
Acta Cryst. (2008). F64, 22-24 [ doi:10.1107/S1744309107060897 ] Overexpression, purification and crystallization of the tetrameric form of SorC sorbitol operon regulatorD. de Sanctis, A. T. Rêgo, D. Marçal, C. E. McVey, M. A. Carrondo and F. J. EnguitaSynopsis: The sorbitol operon regulator from K. pneumoniae has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 3.2 Å. Online 20 December 2007 |
Acta Cryst. (2008). F64, 25-28 [ doi:10.1107/S174430910706160X ] Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine
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Acta Cryst. (2008). F64, 29-31 [ doi:10.1107/S1744309107064391 ] Overproduction, purification, crystallization and preliminary X-ray analysis of the peroxiredoxin domain of a larger natural hybrid protein from Thermotoga maritimaC. Barbey, N. Rouhier, A. Haouz, A. Navaza and J.-P. JacquotSynopsis: Crystals of the peroxiredoxin domain of a larger natural hybrid protein from T. maritima were obtained which diffracted to 2.9 Å resolution on a synchrotron source. Online 20 December 2007 |
Acta Cryst. (2008). F64, 32-35 [ doi:10.1107/S1744309107064615 ] Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcisV. Gaur, D. K. Sethi and D. M. SalunkeSynopsis: The purification, identification, crystallization and preliminary crystallographic studies of an allergy-related protein, Pru du amandin, from P. dulcis nuts are reported. Online 20 December 2007 |
Acta Cryst. (2008). F64, 36-38 [ doi:10.1107/S1744309107065256 ] Overproduction, crystallization and preliminary X-ray analysis of the putative L-ascorbate-6-phosphate lactonase UlaG from Escherichia coliF. Garces, F. J. Fernández, R. Pérez-Luque, J. Aguilar, L. Baldomà, M. Coll, J. Badía and M. C. VegaSynopsis: UlaG, the putative L-ascorbate-6-phosphate lactonase encoded by the ulaG gene from the utilization of L-ascorbate regulon in E. coli, has been cloned, overexpressed, purified using standard chromatographic techniques and crystallized in a monoclinic space group. Crystals were obtained by the sitting-drop vapour-diffusion method at 293 K. A data set diffracting to 3 Å resolution was collected from a single crystal at 100 K. Online 20 December 2007 |
Acta Cryst. (2008). F64, 39-43 [ doi:10.1107/S1744309107065372 ] Crystallization and preliminary crystallographic analysis of the catalytic domain of human flap endonuclease 1 in complex with a nicked DNA product: use of a DPCS kit for efficient protein-DNA complex crystallizationS. Sakurai, K. Kitano, H. Morioka and T. HakoshimaSynopsis: Human flap endonuclease 1 complexed with nicked DNA has been crystallized. A diffraction data set was collected to a resolution of 2.75 Å. Online 20 December 2007 |
Acta Cryst. (2008). F64, 44-46 [ doi:10.1107/S1744309107065384 ] Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor
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Acta Cryst. (2008). F64, 47-49 [ doi:10.1107/S1744309107065645 ] Preliminary X-ray crystallographic analysis of SMU.573, a putative sugar kinase from Streptococcus mutansY.-F. Zhou, L.-F. Li, C. Yang, Y.-H. Liang and X.-D. SuSynopsis: SMU.573 from S. mutans was expressed in E. coli and crystallized. The crystals belong to space group I4 and 2.5 Å resolution diffraction data were collected at an in-house chromium radiation source. Online 20 December 2007 |
Acta Cryst. (2008). F64, 50-53 [ doi:10.1107/S1744309107066122 ] Crystallization and preliminary crystallographic studies of an active-site mutant hydantoin racemase from Sinorhizobium meliloti CECT4114S. Martínez-Rodríguez, L. A. González-Ramírez, J. M. Clemente-Jiménez, F. Rodríguez-Vico, F. J. Las Heras-Vázquez, J. A. Gavira and J. M. García-RuizSynopsis: Crystals of an active-site mutated hydantoin racemase from S. meliloti have been obtained in the presence and absence of D,L-5-isopropyl-hydantoin and characterized by X-ray diffraction. Online 20 December 2007 |
Acta Cryst. (2008). F64, 54-57 [ doi:10.1107/S1744309107066444 ] Cleaved thioredoxin fusion protein enables the crystallization of poorly soluble ER
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Acta Cryst. (2008). F64, 58-61 [ doi:10.1107/S1744309107066821 ] Crystallization and preliminary X-ray analysis of Acetivibrio cellulolyticus cellulosomal type II cohesin module: two versions having different linker lengthsI. Noach, O. Alber, E. A. Bayer, R. Lamed, M. Levy-Assaraf, L. J. W. Shimon and F. FrolowSynopsis: The cloning, expression, purification, crystallization and preliminary X-ray characterization of two protein constructs of the second type II cohesin module from A. cellulolyticus ScaB are described. Both constructs contain the native N-terminal linker, but only one of them contains the full-length 45-residue C-terminal linker; the other contains a five-residue segment of this linker. Online 20 December 2007 |
Acta Cryst. (2008). F64, 62 [ doi:10.1107/S1744309107065566 ]
Synopsis: A correction is made to the article by Kefala & Weiss [(2006), Acta Cryst. F62, 1116-1119].
Online 20 December 2007
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