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Cover illustration: Catalytic domain of Streptococcus pneumoniae sialidase NanA (Xu et al., p. 772). |
Acta Cryst. (2008). F64, 772-775 [ doi:10.1107/S1744309108024044 ] Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanAG. Xu, X. Li, P. W. Andrew and G. L. TaylorSynopsis: The structure of a catalytically active subdomain of the NanA sialidase from S. pneumoniae is reported to a resolution of 2.5 Å. The complex with the inhibitor Neu5Ac2en identifies the key catalytic residues and provides a platform for structure-based development of specific inhibitors. PDB reference: 2vvz Online 20 August 2008 |
Acta Cryst. (2008). F64, 776-780 [ doi:10.1107/S1744309108025359 ] Structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal formJ. Vitali and M. J. ColaneriSynopsis: The structure of the catalytic subunit of M. jannaschii aspartate transcarbamoylase has been determined in space group P212121 using synchrotron data to a resolution of 3.0 Å and was refined to a final Rwork and Rfree of 0.215 and 0.269, respectively. PDB reference: 3e2p Online 20 August 2008 |
Acta Cryst. (2008). F64, 781-784 [ doi:10.1107/S174430910802294X ] Purification, crystallization and preliminary X-ray analysis of human mannose-binding lectin-associated serine protease-1 (MASP-1) catalytic regionJ. Dobó, V. Harmat, E. Sebestyén, L. Beinrohr, P. Závodszky and P. GálSynopsis: Acidic nondenaturing PAGE revealed inhomogeneity of the MASP-1 catalytic region caused by deamidation as the reason behind previous unsuccessful crystallization attempts. Monitoring the separation of the various species by acidic nondenaturing PAGE during purification helped to obtain pure protein, which was subsequently crystallized. Online 9 August 2008 |
Acta Cryst. (2008). F64, 785-787 [ doi:10.1107/S1744309108023336 ] Expression, purification, crystallization and preliminary X-ray studies of histamine dehydrogenase from Nocardioides simplexT. M. Reed, H. Hirakawa, M. Mure, E. E. Scott and J. LimburgSynopsis: Histamine dehydrogenase from Nocardioides simplex has been expressed, purified and crystallized with full incorporation of 6-S-cysteinyl-FMN. Diffraction data have been collected to 2.7 Å resolution; the crystals belonged to the orthorhombic space group P212121. Online 9 August 2008 |
Acta Cryst. (2008). F64, 788-791 [ doi:10.1107/S1744309108023439 ] Expression, purification, crystallization and preliminary X-ray studies of a prolyl-4-hydroxylase protein from Bacillus anthracisM. A. Miller, E. E. Scott and J. LimburgSynopsis: Prolyl-4-hydroxylase from B. anthracis has been cloned, expressed and crystallized. A complete MAD data set has been collected to 1.4 Å resolution. Online 9 August 2008 |
Acta Cryst. (2008). F64, 792-796 [ doi:10.1107/S174430910802352X ] Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: a putative cytoplasmic ferri-siderophore reductaseV. A. Bamford, M. Armour, S. A. Mitchell, M. Cartron, S. C. Andrews and K. A. WatsonSynopsis: Crystallization of the proposed FAD-containing ferri-siderophore reductase protein YqjH from E. coli has been performed and the structure has been determined to 3.0 Å resolution. The structure shows similarity to another proposed siderophore-interacting protein from S. putrefaciens and weak similarity to members of the NAD(P)H:flavin oxidoreductase superfamily. Online 9 August 2008 |
Acta Cryst. (2008). F64, 797-801 [ doi:10.1107/S1744309108024068 ] Crystallization and preliminary X-ray analysis of CrgA, a LysR-type transcriptional regulator from pathogenic Neisseria meningitidis MC58S. Sainsbury, J. Ren, N. J. Saunders, D. I. Stuart and R. J. OwensSynopsis: The full length and the regulatory domain of the LysR-type transcriptional regulator CrgA have been crystallized. Diffraction data were collected from two crystal forms of full-length CrgA to 3.0 and 3.8 Å resolution, respectively. Crystals of the selenomethionine derivative of the C-terminal regulatory domain of CrgA diffracted to 2.3 Å resolution. Online 9 August 2008 |
Acta Cryst. (2008). F64, 802-804 [ doi:10.1107/S1744309108024391 ] Purification, crystallization and preliminary crystallographic analysis of avian infectious bronchitis virus nsp3 ADRP domainL. Wei, C. Chen, Q. Zhao, C. Li, L. Cong, X. Xu, Y. Ma, M. Liao, Y. Xu and Z. RaoSynopsis: The crystal of the nsp3 ADRP domain of avian infectious bronchitis virus (IBV) has been obtained and subjected to further crystallograghic studies. Online 9 August 2008 |
Acta Cryst. (2008). F64, 805-808 [ doi:10.1107/S1744309108024500 ] Expression, purification and preliminary crystallographic analysis of N-acetylglucosamine-1-phosphate uridylyltransferase from Mycobacterium tuberculosisJ. Yin, C. R. Garen, M. M. Cherney, L. T. Cherney and M. N. G. JamesSynopsis: N-Acetylglucosamine 1-phosphate uridyltransferase (GlmU) from M. tuberculosis H37Rv has been crystallized and preliminary X-ray crystallographic analysis has been performed. GlmU is a bi-domained bifunctional enzyme that is involved in the biosynthesis of UDP-N-acetylglucosamine, a precursor in peptidoglycan biosynthesis in M. tuberculosis. Online 9 August 2008 |
Acta Cryst. (2008). F64, 809-812 [ doi:10.1107/S1744309108024731 ] Crystallization and preliminary X-ray diffraction analysis of the peptidylprolyl isomerase Par27 of Bordetella pertussisA. Wohlkönig, H. Hodak, B. Clantin, M. Sénéchal, C. Bompard, F. Jacob-Dubuisson and V. VilleretSynopsis: Par27 from B. pertussis, the prototype of a new group of parvulins has been crystallized in two different crystal forms. Online 9 August 2008 |
Acta Cryst. (2008). F64, 813-815 [ doi:10.1107/S1744309108019283 ] Crystallization and preliminary crystallographic analysis of Gibberella zeae extracellular lipaseY. Sun, M. Li, Y. Zhang, L. Liu, Y. Liu, Z. Liu, X. Li and Z. LouSynopsis: G. zeae extracellular lipase has been overexpressed, purified and crystallized. Diffraction data were collected to 2.8 Å resolution. Online 20 August 2008 |
Acta Cryst. (2008). F64, 816-818 [ doi:10.1107/S1744309108019891 ] Crystallization and preliminary X-ray diffraction studies of the calcium-binding protein CalD from Streptomyces coelicolorX. Zhao, S. Wang, H. Pang, K. Yang and M. BartlamSynopsis: The calcium-binding protein encoded by the CalD gene in S. coelicolor A3(2) has been crystallized as a prelude towards the determination of its three-dimensional structure by X-ray crystallography. Online 20 August 2008 |
Acta Cryst. (2008). F64, 819-821 [ doi:10.1107/S174430910802277X ] Crystallographic study of G178S mutant of human proliferating cell nuclear antigenA. Hishiki, T. Shimizu, A. Serizawa, H. Ohmori, M. Sato and H. HashimotoSynopsis: Crystallization and diffraction studies of human PCNA G178S mutant are reported. Online 20 August 2008 |
Acta Cryst. (2008). F64, 822-824 [ doi:10.1107/S1744309108025086 ] Crystallization and preliminary crystallographic analysis of the complex of the second and third regulatory subunits of human Pol
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Acta Cryst. (2008). F64, 825-827 [ doi:10.1107/S1744309108025128 ] Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine
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Acta Cryst. (2008). F64, 828-830 [ doi:10.1107/S1744309108025384 ] Crystallization and preliminary X-ray diffraction analysis of L-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensisA. Bowyer, H. Mikolajek, J. N. Wright, A. Coker, P. T. Erskine, J. B. Cooper, Q. Bashir, N. Rashid, F. Jamil and M. AkhtarSynopsis: The L-threonine dehydrogenase from T. kodakaraensis KOD1 has been crystallized in the tetragonal space group P43212, with unit-cell parameters a = b = 124.5, c = 271.1 Å. Diffraction data were collected to 2.6 Å resolution and preliminary analysis indicates that there are four molecules in the crystallographic asymmetric unit. Online 20 August 2008 |
Acta Cryst. (2008). F64, 831-835 [ doi:10.1107/S1744309108025426 ] Purification and crystallization of a non-GluR2 AMPA-receptor ligand-binding domain: a case of cryo-incompatibility addressed by room-temperature data collectionA. Gill and D. R. MaddenSynopsis: High-resolution diffraction was obtained from GluR4 AMPA-receptor ligand-binding domain crystals using a combination of cryogenic and room-temperature data-collection strategies. Online 20 August 2008 |
Acta Cryst. (2008). F64, 836-839 [ doi:10.1107/S1744309108025487 ] Coenzyme- and His-tag-induced crystallization of octopine dehydrogenaseS. H. J. Smits, A. Mueller, M. K. Grieshaber and L. SchmittSynopsis: The crystal structure of octopine dehydrogenase revealed a specific role of the His5 tag in inducing the crystal contacts required for successful crystallization. Online 20 August 2008 |
Acta Cryst. (2008). F64, 840-846 [ doi:10.1107/S174430910802558X ] Cloning, expression, purification, crystallization and preliminary X-ray analysis of the human RuvBL1-RuvBL2 complexS. Gorynia, P. M. Matias, T. M. Bandeiras, P. Donner and M. A. CarrondoSynopsis: A truncated variant of the human RuvBL1-RuvBL2 complex was cloned, expressed, purified and crystallised. Synchrotron diffraction data to 4 Å resolution were used to carry out a preliminary crystallographic analysis of the complex. Online 20 August 2008 |
Acta Cryst. (2008). F64, 847-850 [ doi:10.1107/S174430910802575X ] Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of hypothetical protein SCO4226 from Streptomyces coelicolor A3(2)S. Wang, Y.-X. He, R. Bao, Y.-B. Teng, B.-P. Ye and C.-Z. ZhouSynopsis: A hypothetical protein SCO4226 from S. coelicolor has been overexpressed, purified and crystallized. The crystals belonged to space group P21 and diffracted to 2.0 Å resolution. Online 20 August 2008 |
Acta Cryst. (2008). F64, 851-853 [ doi:10.1107/S1744309108025840 ] Crystallization and preliminary X-ray crystallographic study of flavoredoxin from Desulfovibrio vulgaris Miyazaki FY. Ueda, N. Shibata, D. Takeuchi, M. Kitamura and Y. HiguchiSynopsis: Flavoredoxin from D. vulgaris Miyazaki F has been purified and crystallized. The crystals diffracted to 1.05 Å resolution using synchrotron radiation. Online 20 August 2008 |
Acta Cryst. (2008). F64, 854-857 [ doi:10.1107/S1744309108025979 ] Crystallization and X-ray analysis of the Schistosoma mansoni guanidino kinaseA. M. Awama, P. Paracuellos, S. Laurent, C. Dissous, O. Marcillat and P. GouetSynopsis: The X-ray structure of the guanidino kinase from S. mansoni has been determined at 2.8 Å resolution by the molecular-replacement method. Online 20 August 2008 |
Acta Cryst. (2008). F64, 858-862 [ doi:10.1107/S1744309108026596 ] Screening of detergents for solubilization, purification and crystallization of membrane proteins: a case study on succinate:ubiquinone oxidoreductase from Escherichia coliH. Shimizu, C. Nihei, D. K. Inaoka, T. Mogi, K. Kita and S. HaradaSynopsis: Succinate:ubiquinone oxidoreductase was solubilized and purified from E. coli inner membranes using several different detergents and the phospholipid content of each preparation was analyzed. The preparation with the lowest phospholipid content crystallized in two different crystal forms using detergent mixtures composed of n-alkyl-oligoethylene glycol monoether and n-alkyl-maltoside. Online 29 August 2008 |
Acta Cryst. (2008). F64, 863-866 [ doi:10.1107/S1744309108026559 ] Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of tetrahydrodipicolinate-N-succinyltransferase (Rv1201c) from Mycobacterium tuberculosisL. Schuldt, S. Weyand, G. Kefala and M. S. WeissSynopsis: M. tuberculosis tetrahydrodipicolinate-N-succinyltransferase, the enzyme that catalyses the fifth reaction step of the lysine-biosynthesis pathway, has been cloned, expressed, purified and crystallized. Online 29 August 2008 |
Acta Cryst. (2008). F64, 867-869 [ doi:10.1107/S1744309108026535 ] Crystallographic characterization of the N-terminal domain of a plant NADPH oxidaseT. Oda, H. Hashimoto, N. Kuwabara, K. Hayashi, C. Kojima, T. Kawasaki, K. Shimamoto, M. Sato and T. ShimizuSynopsis: A crystal of the N-terminal domain of a plant NADPH oxidase was obtained and X-ray diffraction data were collected on a synchrotron beamline to a maximum resolution of 2.4 Å. Online 29 August 2008 |
Acta Cryst. (2008). F64, 870-874 [ doi:10.1107/S174430910802678X ] Rational `correction' of the amino-acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallizationM. Tarnawski, S. Krzywda, A. Szczepaniak and M. JaskolskiSynopsis: Recombinant RuBisCO chaperone from T. elongatus, TeRbcX, was aggregated and could not be crystallized. Mutations of an unusual Cys residue in the TeRbcX sequence yielded much better behaved proteins that could rapidly be crystallized. Online 29 August 2008 |
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