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Cover illustration: A putative molybdenum-cofactor biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472) (Yoshida et al., p. 589). |
Acta Cryst. (2008). F64, 572-576 [ doi:10.1107/S1744309108015212 ] Structure of Ynk1 from the yeast Saccharomyces cerevisiaeH. Wang, R. Bao, C. Jiang, Z. Yang, C.-Z. Zhou and Y. ChenSynopsis: The crystal structure of Ynk1, an NDPK from the yeast Saccharomyces cerevisiae, has been solved at 3.1 Å resolution. PDB reference: 3b54 Online 28 June 2008 |
Acta Cryst. (2008). F64, 577-583 [ doi:10.1107/S174430910801556X ] Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromineD. B. Langley, D. M. Trambaiolo, A. P. Duff, D. M. Dooley, H. C. Freeman and J. M. GussSynopsis: The structures of complexes of the copper-containing amine oxidase from A. globiformis with benzylhydrazine and tranylcypromine have been refined at 1.86 and 1.65 Å resolution, respectively. Online 11 June 2008 |
Acta Cryst. (2008). F64, 584-588 [ doi:10.1107/S1744309108016035 ] Conformational change of the AcrR regulator reveals a possible mechanism of inductionR. Gu, M. Li, C.-C. Su, F. Long, M. D. Routh, F. Yang, G. McDermott and E. W. YuSynopsis: The crystal structure of Escherichia coli AcrR with space group P31, which is distinct from our previously reported P2221 space-group structure, has been determined. A comparison of these two structures reveals possible mechanisms of ligand binding and AcrR regulation. PDB reference: 3bcg Online 11 June 2008 |
Acta Cryst. (2008). F64, 589-592 [ doi:10.1107/S174430910801590X ] Structure of a putative molybdenum-cofactor biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472)H. Yoshida, M. Yamada, S. Kuramitsu and S. KamitoriSynopsis: The crystal structure of a putative molybdenum-cofactor biosynthesis protein C (MoaC) from S. tokodaii (ST0472) was determined at 2.2 Å resolution. PDB reference: 2ohd Online 11 June 2008 |
Acta Cryst. (2008). F64, 593-595 [ doi:10.1107/S1744309108008816 ] Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774O. Y. Gavel, A. V. Kladova, S. A. Bursakov, J. M. Dias, S. Texeira, V. L. Shnyrov, J. J. G. Moura, I. Moura, M. J. Romão and J. TrincãoSynopsis: Native zinc-containing ATP sulfurylase from D. desulfuricans ATCC 27774 was purified to homogeneity and crystallized. Diffraction data were collected to 2.5 Å resolution. Online 7 June 2008 |
Acta Cryst. (2008). F64, 596-598 [ doi:10.1107/S1744309108008865 ] Purification, crystallization and preliminary crystallographic analysis of DehI, a group I
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Acta Cryst. (2008). F64, 599-601 [ doi:10.1107/S1744309108009251 ] Purification, crystallization and preliminary X-ray crystallographic analysis of Rab27a GTPase in complex with exophilin4/Slp2-a effectorL. M. G. Chavas, K. Ihara, M. Kawasaki, R. Kato, T. Izumi and S. WakatsukiSynopsis: The GppNHp-bound Rab27a GTPase in complex with exophilin4/Slp2-a has been purified and crystallized. Preliminary crystallographic analyses have been performed at 1.8 Å resolution. Online 7 June 2008 |
Acta Cryst. (2008). F64, 602-604 [ doi:10.1107/S1744309108009299 ] Expression, purification and preliminary crystallographic analysis of recombinant human small glutamine-rich tetratricopeptide-repeat proteinS. Dutta, M. Kotaka and Y.-J. TanSynopsis: The production and crystallization of the tetratricopeptide-repeat domain of human small glutamine-rich tetratricopeptide-repeat protein are reported. A 2.4 Å native diffraction data set has been obtained. Online 7 June 2008 |
Acta Cryst. (2008). F64, 605-609 [ doi:10.1107/S1744309108013432 ] Crystallization and preliminary crystallographic analysis of merohedrally twinned crystals of MJ0729, a CBS-domain protein from Methanococcus jannaschiiP. Fernández-Millán, D. Kortazar, M. Lucas, M. L. Martínez-Chantar, E. Astigarraga, J. A. Fernández, O. Sabas, A. Albert, J. M. Mato and L. A. Martínez-CruzSynopsis: Trigonal crystals of MJ0729 showing different degrees of merohedral twinning that may vary from perfect hemihedral twinning to perfect tetartohedral twinning were obtained upon slight variation of the pH. Online 7 June 2008 |
Acta Cryst. (2008). F64, 610-613 [ doi:10.1107/S1744309108014723 ] Crystallization and preliminary X-ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticusM. Nakasako, R. Obata, R. Okubo, S. Nakayama, K. Miyamoto and H. OhtaSynopsis: Crystals of arylmalonate decarboxylase from A. bronchisepticus were obtained which diffracted X-rays to a resolution of at least 3.0 Å. Online 11 June 2008 |
Acta Cryst. (2008). F64, 614-616 [ doi:10.1107/S1744309108015492 ] Nuclear receptor ligand-binding domains: reduction of helix H12 dynamics to favour crystallizationV. Nahoum, A. Lipski, F. Quillard, J.-F. Guichou, Y. Boublik, E. Pérez, P. Germain, A. R. de Lera and W. BourguetSynopsis: Attempts have been made to crystallize the ligand-binding domain of the human retinoid X receptor in complex with a variety of newly synthesized ligands. An inverse correlation was observed between the `crystallizability' and the structural dynamics of the various receptor-ligand complexes. Online 11 June 2008 |
Acta Cryst. (2008). F64, 617-621 [ doi:10.1107/S1744309108015534 ] Crystallization and preliminary X-ray diffraction anaylsis of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thalianaM. Nakasako, M. Hirata, N. Shimizu, S. Hosokawa, D. Matsuoka, T. Oka, M. Yamamoto and S. TokutomiSynopsis: Crystals of the LOV1 domains of phototropin 1 and 2 from A. thaliana were obtained which diffracted X-rays to a resolution of at least 2.1 Å. Online 11 June 2008 |
Acta Cryst. (2008). F64, 622-624 [ doi:10.1107/S1744309108015583 ] Crystallization and preliminary X-ray analysis of a class II release factor RF3 from a sulfate-reducing bacteriumK. Kihira, S. Numata, M. Kitamura, J. Kondo, S. Terawaki, Y. Shomura, H. Komori, N. Shibata and Y. HiguchiSynopsis: Class II release factor 3 (RF3) from the sulfate-reducing bacterium D. vulgaris Miyazaki F has been overexpressed, purified and crystallized in complex with GDP. Online 11 June 2008 |
Acta Cryst. (2008). F64, 625-628 [ doi:10.1107/S1744309108015728 ] Improvement of the quality of lumazine synthase crystals by protein engineeringL. Rodríguez-Fernández, F. J. López-Jaramillo, A. Bacher, M. Fischer and S. WeinkaufSynopsis: Site-directed mutagenesis has been applied to improve the overexpression and purification of the icosahedral enzyme lumazine synthase from B. subtilis as well as to produce a new crystal form. The mutant protein crystallizes in space group R3 and diffracts X-rays to 1.6 Å resolution. Online 11 June 2008 |
Acta Cryst. (2008). F64, 629-631 [ doi:10.1107/S1744309108016059 ] Crystallization and preliminary X-ray characterization of the genetically encoded fluorescent calcium indicator protein GCaMP2M. M. Rodríguez Guilbe, E. C. Alfaro Malavé, J. Akerboom, J. S. Marvin, L. L. Looger and E. R. SchreiterSynopsis: The genetically encoded fluorescent calcium-indicator protein GCaMP2 was crystallized in the calcium-saturated form. X-ray diffraction data were collected to 2.0 Å resolution and the structure was solved by molecular replacement. Online 11 June 2008 |
Acta Cryst. (2008). F64, 632-635 [ doi:10.1107/S1744309108016278 ] Crystallization and preliminary X-ray diffraction studies of a novel ferredoxin involved in the dioxygenation of carbazole by Novosphingobium sp. KA1T. Umeda, J. Katsuki, Y. Usami, K. Inoue, H. Noguchi, Z. Fujimoto, Y. Ashikawa, H. Yamane and H. NojiriSynopsis: The ferredoxin component of carbazole 1,9a-dioxygenase (CARDO-F) is involved in an electron-transfer reaction. The CARDO-F from Novosphingobium sp. KA1 was crystallized under anaerobic conditions and diffracted to a resolution of 1.9 Å. Online 11 June 2008 |
Acta Cryst. (2008). F64, 636-638 [ doi:10.1107/S1744309108016321 ] Overproduction, crystallization and preliminary X-ray characterization of Abn2, an endo-1,5-
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Acta Cryst. (2008). F64, 639-640 [ doi:10.1107/S1744309108016928 ] Crystallization and crystallographic analysis of human NUDT16J. Zhang, F. Gao, Q. Zhang, Q. Chen, J. Qi and J. YanSynopsis: Recombinant NUDT16 from human was expressed, purified and crystallized. The native crystals diffracted to 2.1 Å. Online 11 June 2008 |
Acta Cryst. (2008). F64, 641-644 [ doi:10.1107/S1744309108016242 ] Purification, crystallization and initial crystallographic characterization of the Ginkgo biloba 11S seed globulin ginnacinT. Jin, Y.-W. Chen, A. Howard and Y.-Z. ZhangSynopsis: The crystallization of ginnacin, the 11S seed storage protein from G. biloba, is reported. Online 28 June 2008 |
Acta Cryst. (2008). F64, 645-647 [ doi:10.1107/S1744309108016394 ] Crystallization, X-ray diffraction analysis and preliminary structure determination of the polygalacturonase PehA from Agrobacterium vitisP. B. Vordtriede and M. D. YoderSynopsis: The acidic polygalacturonase PehA from A. vitis has been crystallized. A molecular-replacement solution indicated a right-handed parallel Online 28 June 2008 |
Acta Cryst. (2008). F64, 648-650 [ doi:10.1107/S1744309108016552 ] Crystallization and preliminary X-ray crystallographic studies of a PduO-type ATP:cob(I)alamin adenosyltransferase from Bacillus cereusA. K. Park, J. H. Moon, S. H. Lee and Y. M. ChiSynopsis: Orthorhombic crystals of a PduO-type ATP:cob(I)alamin adenosyltransferase from B. cereus were obtained both as an apoenzyme and in the presence of Mg2+ and ATP. Online 28 June 2008 |
Acta Cryst. (2008). F64, 651-655 [ doi:10.1107/S174430910801676X ] Crystallization and preliminary X-ray crystallographic studies of human voltage-dependent anion channel isoform I (HVDAC1)T. Meins, C. Vonrhein and K. ZethSynopsis: The human voltage-dependent anion channel was overproduced in bacteria and refolded with the help of detergents. Extensive screening of crystallization conditions resulted in the first crystals to be obtained of this voltage-dependent anion-channel type. The crystals diffracted to a resolution of 3.6 Å. Online 28 June 2008 |
Acta Cryst. (2008). F64, 656-658 [ doi:10.1107/S1744309108016734 ] Cloning, purification and preliminary crystallographic analysis of a putative DNA-binding membrane protein, YmfM, from Staphylococcus aureusL. Xu, S. E. Sedelnikova, P. J. Baker and D. W. RiceSynopsis: Truncation by the removal of the C-terminal hydrophobic transmembrane anchor has enabled the overexpression of a soluble domain of S. aureus YmfM in Escherichia coli, which has then been purified and subsequently crystallized. Online 28 June 2008 |
Acta Cryst. (2008). F64, 659-661 [ doi:10.1107/S1744309108016746 ] Purification, crystallization and preliminary X-ray diffraction studies to near-atomic resolution of dihydrodipicolinate synthase from methicillin-resistant Staphylococcus aureusB. R. Burgess, R. C. J. Dobson, C. Dogovski, G. B. Jameson, M. W. Parker and M. A. PeruginiSynopsis: Dihydrodipicolinate synthase (DHDPS), an enzyme of the lysine-biosynthetic pathway, is a promising target for antibiotic development against pathogenic bacteria. Here, the expression, purification, crystallization and preliminary diffraction analysis to 1.45 Å resolution of DHDPS from methicillin-resistant S. aureus is reported. Online 28 June 2008 |
Acta Cryst. (2008). F64, 662-664 [ doi:10.1107/S1744309108016849 ] Purification, crystallization and preliminary X-ray analysis of urease from pigeon pea (Cajanus cajan)A. Balasubramanian and K. PonnurajSynopsis: Urease from pigeon pea was purified and crystallized and X-ray diffraction data were collected at 2.5 Å resolution. Online 28 June 2008 |
Acta Cryst. (2008). F64, 665-667 [ doi:10.1107/S1744309108017405 ] Crystallization and preliminary X-ray diffraction analysis of mouse galectin-4 N-terminal carbohydrate recognition domain in complex with lactoseV. Krejciríková, M. Fábry, V. Marková, P. Malý, P. Rezácová and J. BryndaSynopsis: Mouse galectin-4 carbohydrate binding domain was overexpressed in E. coli and crystallized in the presence of lactose. The crystals belong to tetragonal space group P4212 and diffraction data were collected to 2.1 Å resolution. Online 28 June 2008 |
Acta Cryst. (2008). F64, 668-670 [ doi:10.1107/S1744309108017545 ] Crystallization and preliminary X-ray analysis of allene oxide synthase, cytochrome P450 CYP74A2, from Parthenium argentatumZ. Chang, L. Li, Z. Pan and X. WangSynopsis: Allene oxide synthase, an atypical cytochrome P450 from Parthenium argentatum, was crystallized and diffraction data were collected to 2.4 Å resolution. Online 28 June 2008 |
Acta Cryst. (2008). F64, 671-673 [ doi:10.1107/S1744309108017703 ] Purification, crystallization and preliminary crystallographic studies of plant S-adenosyl-L-homocysteine hydrolase (Lupinus luteus)K. Brzezinski, G. Bujacz and M. JaskolskiSynopsis: Single crystals of recombinant S-adenosyl-L-homocysteine hydrolase from L. luteus in complex with adenosine diffract X-rays to 1.17 Å resolution at 100 K. The crystals are tetragonal, space group P43212, and contain one copy of the dimeric enzyme in the asymmetric unit. Online 28 June 2008 |
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