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Cover illustration: A selection of the best crystal pictures published in Acta Cryst. F during the past year. |
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Acta Cryst. (2012). F68, 1 [ doi:10.1107/S1744309111053759 ] Crystals on the cover 2012H. Einspahr and M. S. WeissSynopsis: Editorial. Online 24 December 2011 |
Acta Cryst. (2012). F68, 2-7 [ doi:10.1107/S1744309111048056 ] Structural insights into RipC, a putative citrate lyase
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Acta Cryst. (2012). F68, 8-13 [ doi:10.1107/S174430911104807X ] Structure of CBM3b of the major cellulosomal scaffoldin subunit ScaA from Acetivibrio cellulolyticusO. Yaniv, Y. Halfon, L. J. W. Shimon, E. A. Bayer, R. Lamed and F. FrolowSynopsis: The crystal structure at 1.0 Å resolution of the cellulose-binding CBM3b from the major scaffoldin subunit ScaA of A. cellulolyticus is described. PDB references: 3zqw, 3zuc and 3zu8 Online 24 December 2011 |
Acta Cryst. (2012). F68, 14-19 [ doi:10.1107/S1744309111048184 ] Structure of N-formylglycinamide ribonucleotide amidotransferase II (PurL) from Thermus thermophilus HB8S. Suzuki, H. Yanai, M. Kanagawa, S. Tamura, Y. Watanabe, K. Fuse, S. Baba, G. Sampei and G. KawaiSynopsis: The structure of PurL from T. thermophilus HB8 in complex with an adenine nucleotide is reported at 2.35 Å resolution. PDB reference: 3viu Online 24 December 2011 |
Acta Cryst. (2012). F68, 20-23 [ doi:10.1107/S1744309111038139 ] Expression, refolding and preliminary X-ray crystallographic analysis of equine MHC class I molecule complexed with an EIAV-Env CTL epitopeS. Yao, J. Qi, J. Liu, R. Chen, X. Pan, X. Li, F. Gao and C. XiaSynopsis: The equine MHC class I molecule was crystallized in complex with Online 24 December 2011 |
Acta Cryst. (2012). F68, 24-31 [ doi:10.1107/S1744309111048020 ] Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profileE. Dall and H. BrandstetterSynopsis: The enzymatic activation of human legumain requires both proteolytic cleavage and conformational reordering and is modulated by its substrate as well as cofactors. These biochemical findings are aided by the crystallization and initial crystallographic analysis of legumain. Online 24 December 2011 |
Acta Cryst. (2012). F68, 32-36 [ doi:10.1107/S1744309111045386 ] Molecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction studies of histidinol phosphate aminotransferase (HisC2) from Mycobacterium tuberculosisN. Nasir, R. Vyas, C. Chugh, M. S. Ahangar and B. K. BiswalSynopsis: HisC2 from M. tuberculosis was cloned, overexpressed, purified and crystallized and the crystals were characterized. Online 24 December 2011 |
Acta Cryst. (2012). F68, 37-40 [ doi:10.1107/S1744309111044708 ] Crystallization and preliminary X-ray crystallographic analysis of the membrane-binding haemprotein nitrophorin 7 from Rhodnius prolixusH. Ogata and M. KnippSynopsis: The crystallization of recombinant nitrophorin 7 originating from the bloodsucking insect R. prolixus is described. The crystals diffracted to 1.8 Å resolution. Online 24 December 2011 |
Acta Cryst. (2012). F68, 41-44 [ doi:10.1107/S1744309111046318 ] Protein expression, crystallization and preliminary X-ray crystallographic analysis of chicken interferon-
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Acta Cryst. (2012). F68, 45-48 [ doi:10.1107/S1744309111045842 ] Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of Cockayne syndrome protein A in complex with DNA damage-binding protein 1E. M. Meulenbroek and N. S. PannuSynopsis: Human Cockayne syndrome protein A has been cocrystallized with human DNA damage-binding protein 1 and data have been collected to 2.9 Å resolution. Online 24 December 2011 |
Acta Cryst. (2012). F68, 49-52 [ doi:10.1107/S1744309111044551 ] Crystallization and preliminary neutron diffraction studies of ADP-ribose pyrophosphatase-I from Thermus thermophilus HB8N. Okazaki, M. Adachi, T. Tamada, K. Kurihara, T. Ooga, N. Kamiya, S. Kuramitsu and R. KurokiSynopsis: ADP-ribose pyrophosphatase-I, a Nudix enzyme, from T. thermophilus was crystallized for neutron diffraction. Neutron and X-ray diffraction data sets were collected to 2.1 and 1.5 Å resolution, respectively. Online 24 December 2011 |
Acta Cryst. (2012). F68, 53-55 [ doi:10.1107/S1744309111046082 ] Crystallization and preliminary X-ray crystallographic studies of the outer membrane cytochrome OmcA from Shewanella oneidensis MR-1S. J. Tomanicek, A. Johs, M. S. Sawhney, L. Shi and L. LiangSynopsis: The purification and crystallization of the outer membrane decaheme c-type cytochrome OmcA from S. oneidensis MR-1 are reported. The plate-like crystals belonged to the monoclinic space group P21 and diffracted to 3.25 Å resolution. Online 24 December 2011 |
Acta Cryst. (2012). F68, 56-58 [ doi:10.1107/S1744309111047099 ] Crystallization and preliminary X-ray crystallographic analysis of the
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Acta Cryst. (2012). F68, 59-62 [ doi:10.1107/S1744309111048068 ] Purification, crystallization and preliminary crystallographic analysis of human dihydrodipicolinate synthase-like protein (DHDPSL)R. D. Bunker, K. M. Loomes and E. N. BakerSynopsis: A human enzyme, DHDPSL, which is homologous to bacterial pyruvate-dependent aldolases but of unknown function, has been expressed, purified and crystallized with the use of in situ proteolysis. The crystals diffracted to 2.0 Å resolution and were suitable for structure determination. Online 24 December 2011 |
Acta Cryst. (2012). F68, 63-65 [ doi:10.1107/S1744309111048111 ] Expression, purification, crystallization and preliminary X-ray crystallographic analysis of L-lactate dehydrogenase and its H171C mutant from Bacillus subtilisY. Zhang and X. GaoSynopsis: Recombinant wild-type L-lactate dehydrogenase from B. subtilis (BsLDH) was cocrystallized with fructose 1,6-bisphosphate and NAD+ and the crystal diffracted to 2.38 Å resolution. The H171C mutant of BsLDH was also crystallized as the apoenzyme and in complex with NAD+ and the crystals diffracted to 2.20 and 2.49 Å, respectively. All crystals belonged to space group P3. Online 24 December 2011 |
Acta Cryst. (2012). F68, 66-68 [ doi:10.1107/S1744309111048688 ] Crystallization and preliminary X-ray analysis of pyridoxine 4-oxidase, the first enzyme in pyridoxine degradation pathway IA. N. Mugo, J. Kobayashi, B. Mikami, K. Ohnishi and T. YagiSynopsis: Recombinant pyridoxine 4-oxidase from M. loti MAFF303099 was crystallized and diffraction data were collected to 2.2 Å resolution. Online 24 December 2011 |
Acta Cryst. (2012). F68, 69-72 [ doi:10.1107/S1744309111047634 ] Purification, crystallization and preliminary X-ray crystallographic analysis of Arabidopsis thaliana dynamin-related protein 1A GTPase-GED fusion proteinX. Chen, X. Xu, Y. Sun, J. Zhou, Y. Ma, L. Yan and Z. LouSynopsis: A. thaliana dynamin-related protein 1A GTPase domain fused with its GTPase effector domain was overexpressed, purified and crystallized in a hexagonal crystal form that diffracted to 3.6 Å resolution. Online 24 December 2011 |
Acta Cryst. (2012). F68, 73-77 [ doi:10.1107/S1744309111047920 ] Expression, purification, crystallization and preliminary X-ray crystallographic analysis of human
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Acta Cryst. (2012). F68, 78-80 [ doi:10.1107/S1744309111049426 ] Crystallization and preliminary X-ray crystallographic studies of a new class of enoyl-(acyl-carrier protein) reductase, FabV, from Vibrio fischeriA. K. Park, J. H. Lee, Y. M. Chi and J. H. MoonSynopsis: An orthorhombic crystal of an enoyl-(acyl-carrier protein) reductase from V. fischeri was obtained and diffraction data were collected to 2.7 Å resolution. Online 24 December 2011 |
Acta Cryst. (2012). F68, 81-84 [ doi:10.1107/S1744309111048743 ] Expression, purification and preliminary structural analysis of the head domain of Deinococcus radiodurans RecNS. Pellegrino, J. Radzimanowski, S. McSweeney and J. TimminsSynopsis: The head domain of the DNA-repair protein RecN from D. radiodurans, composed of the amino- and carboxy-terminal domains, was crystallized. X-ray diffraction data were collected to 3.0 Å resolution and the crystals belonged to space group P21. Online 24 December 2011 |
Acta Cryst. (2012). F68, 85-88 [ doi:10.1107/S1744309111049530 ] Crystallization and preliminary X-ray crystallographic analysis of the plant defensin NaD1F. T. Lay, G. D. Mills, M. D. Hulett and M. KvansakulSynopsis: NaD1 is a potent antifungal plant defensin. Here, the crystallization and preliminary X-ray crystallographic analysis of NaD1 are reported in order to obtain insight into the structural basis of its antifungal activity. Online 24 December 2011 |
Acta Cryst. (2012). F68, 89-92 [ doi:10.1107/S1744309111049529 ] Purification, crystallization and preliminary X-ray diffraction analysis of the IL-20-IL-20R1-IL-20R2 complexN. J. Logsdon, C. E. Allen, K. R. Rajashankar and M. R. WalterSynopsis: The purification and crystallization of the IL-20-IL-20R1-IL-20R2 ternary complex is described. A low-temperature SAD data set was collected using synchrotron radiation, which showed that the crystals belonged to space group P41212 or its enantiomorph P43212 and contained one ternary complex in the asymmetric unit. Online 24 December 2011 |
Acta Cryst. (2012). F68, 93-97 [ doi:10.1107/S174430911105038X ] Expression, purification and preliminary crystallographic studies of NahF, a salicylaldehyde dehydrogenase from Pseudomonas putida G7 involved in naphthalene degradationJ. B. Coitinho, D. M. A. Costa, S. L. Guimarães, A. M. de Góes and R. A. P. NagemSynopsis: NahF is a salicylaldehyde dehydrogenase that is involved in the naphthalene-degradation pathway, converting salicylaldehyde into salicylate. The subcloning, expression, purification and preliminary X-ray diffraction studies at 2.42 Å resolution of P. putida G7 NahF are reported. Online 24 December 2011 |
Acta Cryst. (2012). F68, 98-100 [ doi:10.1107/S1744309111050391 ] Overexpression, crystallization and preliminary X-ray crystallographic analysis of the RNA polymerase domain of primase from Streptococcus mutans strain UA159D.-W. Im, T.-O. Kim, H. Y. Jung, J. E. Oh, S. J. Lee and Y.-S. HeoSynopsis: The RNA polymerase domain of primase from S. mutans strain UA159 was cloned, overexpressed, purified and crystallized. X-ray diffraction data were collected to a resolution of 1.60 Å. Online 24 December 2011 |
Acta Cryst. (2012). F68, 101-104 [ doi:10.1107/S1744309111050597 ] Crystallization and preliminary X-ray data analysis of a DJ-1 homologue from Arabidopsis thaliana (AtDJ-1D)K. H. Seo, N. Zhuang, J.-Y. Cha, D. Son and K. H. LeeSynopsis: A DJ-1 homologue protein from A. thaliana (AtDJ-1D) has been crystallized. Diffraction data were collected to 2.05 Å resolution for structure determination by the multiple-wavelength anomalous dispersion (MAD) method. Online 24 December 2011 |
Acta Cryst. (2012). F68, 105-110 [ doi:10.1107/S1744309111048706 ] Improving the diffraction of apoA-IV crystals through extreme dehydrationX. Deng, W. S. Davidson and T. B. ThompsonSynopsis: Apolipoprotein A-IV crystals consisted of a long unit-cell edge (540 Å) with a high mosaic spread, making them intractable for X-ray diffraction analysis. Extreme dehydration in 60% PEG 3350 was utilized as a post-crystallization treatment as well a screening method to significantly sharpen the mosaic spread and increase the overall resolution of diffraction. Online 24 December 2011 |
Acta Cryst. (2012). F68, 111-114 [ doi:10.1107/S1744309111054029 ] Measurement of the equilibrium relative humidity for common precipitant concentrations: facilitating controlled dehydration experimentsM. J. Wheeler, S. Russi, M. G. Bowler and M. W. BowlerSynopsis: The equilibrium relative humidity values for a number of the most commonly used precipitants in macromolecular crystallization have been measured using a humidity-control device and compared with independent values where available. The results will simplify experiments using the device. Online 24 December 2011 |
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