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Cover illustration: High-resolution structure of proteinase K cocrystallized with digalacturonic acid (Larson et al., p. 192). |
Acta Cryst. (2009). F65, 192-198 [ doi:10.1107/S1744309109002218 ] High-resolution structure of proteinase K cocrystallized with digalacturonic acidS. B. Larson, J. S. Day, C. Nguyen, R. Cudney and A. McPhersonSynopsis: The crystal structure of proteinase K cocrystallized with digalacturonic acid and HEPES was solved at 1.32 Å resolution. The disaccharide was rotationally disordered about a twofold axis, but nonetheless contributed to intermolecular lattice interactions. PDB reference: 3dyb Online 12 February 2009 |
Acta Cryst. (2009). F65, 199-203 [ doi:10.1107/S1744309109002115 ] Structure of a D-tagatose 3-epimerase-related protein from the hyperthermophilic bacterium Thermotoga maritimaH. Sakuraba, K. Yoneda, T. Satomura, R. Kawakami and T. OhshimaSynopsis: The crystal structure of a hyperthermophilic D-tagatose 3-epimerase-related protein with a unique active-site architecture was determined. PDB reference: 2zvr Online 14 February 2009 |
Acta Cryst. (2009). F65, 204-209 [ doi:10.1107/S174430910900414X ] The structure of NMB1585, a MarR-family regulator from Neisseria meningitidisC. E. Nichols, S. Sainsbury, J. Ren, T. S. Walter, A. Verma, D. K. Stammers, N. J. Saunders and R. J. OwensSynopsis: The structure of the MarR-family regulator NMB1585 from N. meningitidis has been solved using data extending to 2.1 Å resolution. PDB reference: 3g3z Online 26 February 2009 |
Acta Cryst. (2009). F65, 210-212 [ doi:10.1107/S1744309109000700 ] Cloning, purification, crystallization and preliminary X-ray analysis of a chimeric NADPH-cytochrome P450 reductaseL. Aigrain, D. Pompon, G. Truan and S. MoréraSynopsis: A 2.5 Å resolution data set was collected from a crystal of a soluble chimeric form of NADPH-cytochrome P450 reductase (CPR) produced using a fusion gene composed of the yeast FMN and the human FAD domains. The chimeric protein was crystallized in a modified conformation compared with the previously solved structures. Online 12 February 2009 |
Acta Cryst. (2009). F65, 213-215 [ doi:10.1107/S1744309109000797 ] Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia boliviana Piper seedsT. R. Moura, G. A. Bezerra, M. J. B. Bezerra, C. S. Teixera, E. H. S. Bezerra, R. G. Benevides, B. A. M. da Rocha, L. A. G. de Souza, P. Delatorre, C. S. Nagano and B. S. CavadaSynopsis: Canavalia boliviana lectin (Cbol) was purified using a Sephadex G-50 column and crystallized in the presence of X-Man by hanging-drop vapour diffusion at 293 K. After optimization, crystals suitable for diffraction were obtained using 0.1 M HEPES pH 7.5 and 3.0 M sodium formate. Online 12 February 2009 |
Acta Cryst. (2009). F65, 216-218 [ doi:10.1107/S174430910900092X ] Purification, crystallization and preliminary X-ray analysis of an aminoacylhistidine dipeptidase (PepD) from Vibrio alginolyticusC.-Y. Chang, Y.-C. Hsieh, T.-Y. Wang, C.-J. Chen and T.-K. WuSynopsis: The aminoacylhistidine dipeptidase encoded by V. alginolyticus pepD has been overexpressed and crystallized. Online 12 February 2009 |
Acta Cryst. (2009). F65, 219-222 [ doi:10.1107/S1744309109001316 ] Crystallization and preliminary crystallographic analysis of thermophilic cellulase from Fervidobacterium nodosum Rt17-B1B. Zheng, W. Yang, Y. Wang, Y. Feng and Z. LouSynopsis: The thermophilic cellulase FnCel5A from F. nodosum Rt17-B1 has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.4 Å resolution for the native enzyme and to 1.7 Å resolution for the selenomethionyl derivative. Online 12 February 2009 |
Acta Cryst. (2009). F65, 223-225 [ doi:10.1107/S1744309109001419 ] Crystallization and data collection of the nucleotide-binding domain of Mg-ATPaseK. O. Håkansson and A. CurovicSynopsis: Recombinant nucleotide-binding domain of E. coli Mg-ATPase was expressed, purified and used to produce crystals that diffracted to 1.53 Å resolution. Online 12 February 2009 |
Acta Cryst. (2009). F65, 226-231 [ doi:10.1107/S1744309109001511 ] Expression, purification and crystallization of class C acid phosphatases from Francisella tularensis and Pasteurella multocidaH. Singh, R. L. Felts, L. Ma, T. J. Malinski, M. J. Calcutt, T. J. Reilly and J. J. TannerSynopsis: Two members of the class C family of bacterial nonspecific acid phosphatases have been cloned, expressed, purified and crystallized. One of the crystal forms exhibited epitaxial twinning. Online 12 February 2009 |
Acta Cryst. (2009). F65, 232-235 [ doi:10.1107/S1744309109002668 ] A preliminary neutron crystallographic study of an A-DNA crystalR. M. F. Leal, S. C. M. Teixeira, M. P. Blakeley, E. P. Mitchell and V. T. ForsythSynopsis: The LADI-III diffractometer at the Institut Laue-Langevin has been used to carry out the first neutron crystallographic study of a DNA oligonucleotide in the A conformation. The crystal size was 0.06 mm3, the smallest ever used successfully for a study of this type. The results provide evidence of unexpected base protonation and illustrate the opportunities that now exist for nucleic acid crystallography using both hydrogenated and perdeuterated oligonucleotides. Online 12 February 2009 |
Acta Cryst. (2009). F65, 236-241 [ doi:10.1107/S1744309109002267 ] Site-specific unglycosylation to improve crystallization of the metabotropic glutamate receptor 3 extracellular domainT. Muto, D. Tsuchiya, K. Morikawa and H. JingamiSynopsis: The site-specific unglycosylated mutant of metabotropic glutamate receptor 3 extracellular domain has been overexpressed, purified, and crystallized. A complete data set has been collected to 2.35 Å resolution. Online 14 February 2009 |
Acta Cryst. (2009). F65, 242-247 [ doi:10.1107/S1744309109001584 ] Crystallization and preliminary X-ray diffraction analyses of several forms of the CfaB major subunit of enterotoxigenic Escherichia coli CFA/I fimbriaeY.-F. Li, S. Poole, F. Rasulova, A. L. McVeigh, S. J. Savarino and D. XiaSynopsis: Three fusion proteins were generated in order to resolve the atomic structure of the CFA/I fimbriae of enterotoxigenic E. coli. CfaEB is a fusion of the minor and major CFA/I subunits, while CfaBB and CfaBBB are tandem fusions of two and three repeats, respectively, of the major subunit. Each protein was crystallized and the crystal structures of each of these fusions were determined successively by the molecular-replacement method using the CfaE crystal structure as an initial phasing model. Online 14 February 2009 |
Acta Cryst. (2009). F65, 248-252 [ doi:10.1107/S1744309108043145 ] Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domainM. G. Rudolph, J. G. Wittmann and D. KlostermeierSynopsis: Two C-terminal fragments of the RNA helicase Hera have been crytallized in three crystal forms, one of which was phased by MAD using a single selenium site. Online 14 February 2009 |
Acta Cryst. (2009). F65, 253-255 [ doi:10.1107/S1744309108039018 ] Crystallization and preliminary X-ray analysis of dihydrodipicolinate synthase from Clostridium botulinum in the presence of its substrate pyruvateS. C. Atkinson, R. C. J. Dobson, J. M. Newman, M. A. Gorman, C. Dogovski, M. W. Parker and M. A. PeruginiSynopsis: Dihydrodipicolinate synthase (DHDPS) catalyzes an important step in lysine biosynthesis. Here, the crystallization and preliminary diffraction analysis to 1.2 Å resolution of DHDPS from C. botulinum in the presence of its substrate pyruvate is reported. Online 14 February 2009 |
Acta Cryst. (2009). F65, 256-259 [ doi:10.1107/S1744309109001389 ] Expression, purification and crystallization of the cofactor-independent monooxygenase SnoaB from the nogalamycin biosynthetic pathwayH. Koskiniemi, T. Grocholski, G. Schneider and J. NiemiSynopsis: The cofactor-independent monooxygenase SnoaB from the nogalamycin-biosynthesis pathway and a designed selenomethionine-substituted double mutant were crystallized in space group P21212. The native enzyme diffracted to a resolution of 2.4 Å. Online 14 February 2009 |
Acta Cryst. (2009). F65, 260-263 [ doi:10.1107/S1744309108043091 ] Expression, purification and preliminary diffraction studies of CmlSR. Latimer, K. Podzelinska, A. Soares, A. Bhattacharya, L. C. Vining, Z. Jia and D. L. ZechelSynopsis: CmlS from S. venezuelae is a flavin-dependent halogenase that is involved in the biosynthesis of the widely used antibiotic chloramphenicol. Here, the crystallization of CmlS and analysis of the initial diffraction data are reported. Online 26 February 2009 |
Acta Cryst. (2009). F65, 264-266 [ doi:10.1107/S1744309109002462 ] Crystallization and preliminary X-ray diffraction analysis of a putative two-domain-type laccase from a metagenomeH. Komori, K. Miyazaki and Y. HiguchiSynopsis: A putative two-domain-type laccase from a metagenome was crystallized using the sitting-drop vapour-diffusion method. Diffraction data were collected to a resolution of 1.7 Å. Online 26 February 2009 |
Acta Cryst. (2009). F65, 267-270 [ doi:10.1107/S1744309109002504 ] Crystallization and preliminary X-ray crystallographic studies of the Z-DNA-binding domain of a PKR-like kinase (PKZ) in complex with Z-DNAD. Kim, H.-Y. Hwang, Y.-G. Kim and K. K. KimSynopsis: The Z-DNA-binding domain of a PKR-like kinase (PKZ) from goldfish was crystallized in complex with d(TCGCGCG)2. The crystals belonged to space group C2 and diffracted to 1.7 Å resolution. Online 26 February 2009 |
Acta Cryst. (2009). F65, 271-274 [ doi:10.1107/S1744309109003595 ] Preliminary crystallographic study of two cuticle-degrading proteases from the nematophagous fungi Lecanicillium psalliotae and Paecilomyces lilacinusF. Ye, L. Liang, Q. Mi, J. Yang, Z. Lou, Y. Sun, Y. Guo, Z. Meng and K. ZhangSynopsis: Two cuticle-degrading proteases Ver112 and PL646 were purified from the nematophagous fungi L. psalliotae and P. lilacinus, respectively. The protease Ver112 and a complex between PL646 and a tetrapeptide inhibitor were crystallized. Diffraction data were collected to 1.65 and 2.2 Å resolution, respectively. Online 26 February 2009 |
Acta Cryst. (2009). F65, 275-278 [ doi:10.1107/S1744309109002887 ] Crystallization and preliminary X-ray analysis of a cohesin-like module from AF2375 of the archaeon Archaeoglobus fulgidusM. Voronov-Goldman, I. Noach, R. Lamed, L. J. W. Shimon, I. Borovok, E. A. Bayer and F. FrolowSynopsis: A cohesin-like module from the hyperthermophilic archaeon A. fulgidus was cloned, expressed, purified and crystallized. X-ray diffraction data were collected to 1.82 Å resolution. Online 26 February 2009 |
Acta Cryst. (2009). F65, 279-281 [ doi:10.1107/S1744309109003777 ] Expression, purification, crystallization and preliminary crystallographic study of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1S. J. Li, Q. Zhao, Q. Zhou and Y. ZhaiSynopsis: Here, the C-terminal domain of the human voltage-gated proton channel Hv1 (C-Hv1) was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. Online 26 February 2009 |
Acta Cryst. (2009). F65, 282-284 [ doi:10.1107/S1744309109003856 ] Preliminary X-ray crystallographic studies of Bacillus subtilis SpeA proteinX.-Y. Liu, J. Lei, X. Liu, X.-D. Su and L. LiSynopsis: In order to further illustrate the catalytic mechanism of arginine decarboxylase by determining the three-dimensional structure of the enzyme the speA gene was amplified from B. subtilis genomic DNA and cloned. The enzyme was expressed in Escherichia coli and purified to homogeneity by nickel-chelation chromatography followed by size-exclusion chromatography. High-quality crystals were obtained using the hanging-drop vapour-diffusion method at 298 K. Online 26 February 2009 |
Acta Cryst. (2009). F65, 285-287 [ doi:10.1107/S174430910900400X ] Cloning, expression, purification and preliminary crystallographic studies of the adenylate/uridylate-rich element-binding protein HuR complexed with its target RNAD. Iyaguchi, M. Yao, I. Tanaka and E. ToyotaSynopsis: An RNA-binding region of human HuR bound to an 11-base RNA fragment has been crystallized. The crystals diffracted to a resolution of 1.8 Å and belonged to space group P212121. Online 26 February 2009 |
Acta Cryst. (2009). F65, 288-290 [ doi:10.1107/S1744309109004138 ] Crystallization and preliminary X-ray analysis of human liver
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Acta Cryst. (2009). F65, 291-294 [ doi:10.1107/S1744309109004217 ] Expression, purification and preliminary X-ray diffraction studies of VERNALIZATION1208-341 from Arabidopsis thalianaG. King, J. M. Hill, J. L. Martin and J. S. MylneSynopsis: A C-terminal fragment of VERNALIZATION1 from A. thaliana, a DNA-binding protein required for the acceleration of flowering in response to prolonged cold treatment, was crystallized. X-ray diffraction data were collected to a resolution of 2.1 Å. Online 26 February 2009 |
Acta Cryst. (2009). F65, 295-298 [ doi:10.1107/S1744309109004461 ] Crystallization and preliminary X-ray analysis of the tumour necrosis factor
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Acta Cryst. (2009). F65, 299-303 [ doi:10.1107/S1744309109005016 ] Purification, crystallization and preliminary X-ray diffraction of wild-type and mutant recombinant human transforming growth factor
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Acta Cryst. (2009). F65, 304-306 [ doi:10.1107/S1744309109005545 ] Expression, crystallization and preliminary crystallographic analysis of PilZXAC1133 from Xanthomonas axonopodis pv. citriC. R. Guzzo and C. S. FarahSynopsis: The cloning and expression of recombinant PilZXAC1133, a protein belonging to the PilZ superfamily, are described. PilZ proteins are associated with the control of several complex behaviours in bacteria and in some cases have been shown to bind c-diGMP. PilZXAC1133 containing selenomethionine produced crystals that diffracted to 1.85 Å resolution. Online 26 February 2009 |
Acta Cryst. (2009). F65, 307-309 [ doi:10.1107/S1744309109005533 ] Crystallization and preliminary X-ray analysis of LipL32 from Leptospira interrogans serovar CopenhageniP. Hauk, C. R. Guzzo, P. L. Ho and C. S. FarahSynopsis: Recombinant selenomethionine-labelled LipL32, the major surface protein of pathogenic Leptospira, has been purified and crystallized. Data sets from two crystals were collected, one of which diffracted to 2.25 Å resolution. Online 26 February 2009 |
Acta Cryst. (2009). F65, 310-312 [ doi:10.1107/S1744309109005442 ] Purification, crystallization and preliminary crystallographic analysis of Est-Y29: a novel oligomeric
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Acta Cryst. (2009). F65, 313-316 [ doi:10.1107/S1744309109004503 ] Purification, crystallization and preliminary crystallographic study of low oxygen-affinity haemoglobin from cat (Felis silvestris catus) in two different crystal formsM. Balasubramanian, P. S. Moorthy, K. Neelagandan and M. N. PonnuswamySynopsis: Preliminary studies were carried out to purify and crystallize the sample from cat (Felis silvestris catus), a low oxygen-affinity haemoglobin in different crystal forms. Online 26 February 2009 |
Acta Cryst. (2009). F65, 317-320 [ doi:10.1107/S1744309109006630 ] A preliminary neutron diffraction study of
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