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Cover illustration: Escherichia coli malate dehydrogenase at 1.45 Å resolution (Zaitseva, Meneely & Lamb, p. 866). |
Acta Cryst. (2009). F65, 857-861 [ doi:10.1107/S1744309109029674 ] The structure of phosphate-bound Escherichia coli adenylosuccinate lyase identifies His171 as a catalytic acidG. Kozlov, L. Nguyen, J. Pearsall and K. GehringSynopsis: Here, the crystal structure of adenylosuccinate lyase from Escherichia coli was determined to 1.9 Å resolution. PDB reference: 3gzh Online 20 August 2009 |
Acta Cryst. (2009). F65, 862-865 [ doi:10.1107/S1744309109030826 ] Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonateA. Brzuszkiewicz, E. Nowak, Z. Dauter, M. Dauter, H. Cieslinski, A. Dlugolecka and J. KurSynopsis: The crystal structure of the esterase EstA from a cold-adapted bacterium was determined in a form that was covalently inhibited by monoethylphosphonate. PDB reference: 3hp4 Online 20 August 2009 |
Acta Cryst. (2009). F65, 866-869 [ doi:10.1107/S1744309109032217 ] Structure of Escherichia coli malate dehydrogenase at 1.45 Å resolutionJ. Zaitseva, K. M. Meneely and A. L. LambSynopsis: The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 Å resolution. PDB reference: 3hhp Online 20 August 2009 |
Acta Cryst. (2009). F65, 870-873 [ doi:10.1107/S1744309109014997 ] Expression, purification, crystallization and preliminary X-ray analysis of the N-terminal domain of GNBP3 from Drosophila melanogasterY. Mishima, F. Coste, V. Bobezeau, N. Hervouet, C. Kellenberger and A. RousselSynopsis: Crystals of the N-terminal domain of Gram-negative bacteria-binding protein 3 of D. melanogaster grown from PEG solutions are monoclinic (space group C2) and diffract to 1.7 Å resolution. Online 20 August 2009 |
Acta Cryst. (2009). F65, 874-877 [ doi:10.1107/S1744309109030371 ] Crystallization and preliminary X-ray analysis of
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Acta Cryst. (2009). F65, 878-880 [ doi:10.1107/S1744309109028978 ] Crystallization and preliminary X-ray analysis of the small subunit (R2F) of native ribonucleotide reductase from Corynebacterium ammoniagenesH. Ogata, P. Stolle, M. Stehr, G. Auling and W. LubitzSynopsis: The crystallization of the metallo-cofactor (R2F) of native ribonucleotide reductase isolated from the Mn-requiring Gram-positive bacterium C. ammoniagenes is described. The crystals diffracted to 1.36 Å resolution. Online 20 August 2009 |
Acta Cryst. (2009). F65, 881-885 [ doi:10.1107/S1744309109029145 ] Crystallization and preliminary X-ray diffraction data of an LNA 7-mer duplex derived from a ricin aptamerC. Förster, D. Oberthuer, J. Gao, A. Eichert, F. G. Quast, C. Betzel, A. Nitsche, V. A. Erdmann and J. P. FürsteSynopsis: An all-LNA duplex was designed from the stem region of an RNA aptamer which has been generated against ricin. The LNA duplex was crystallized and preliminary X-ray diffraction analysis revealed diffraction to a resolution of up to 2.8 Å. Online 22 August 2009 |
Acta Cryst. (2009). F65, 886-889 [ doi:10.1107/S1744309109028772 ] Crystallization and preliminary X-ray analysis of 4-pyridoxolactonase from Mesorhizobium lotiS. Matsuda, N. Yokochi, Y. Yoshikane, J. Kobayashi, C. N. Huy, S. Baba, S. Kuramitsu, B. Mikami and T. YagiSynopsis: Recombinant 4-pyridoxolactonase from M. loti MAFF303099 was crystallized in two forms and diffraction data were collected to 2.0 and 1.9 Å resolution, respectively. Online 22 August 2009 |
Acta Cryst. (2009). F65, 890-894 [ doi:10.1107/S1744309109029376 ] Crystallization and preliminary X-ray diffraction analysis of motif N from Saccharomyces cerevisiae Dbf4L. A. Matthews, A. Duong, A. A. Prasad, B. P. Duncker and A. GuarnéSynopsis: To understand the role of the Cdc7-Dbf4 complex in checkpoint responses, a fragment of Saccharomyces cerevisiae Dbf4 encompassing motif N was isolated, overproduced and crystallized. Online 22 August 2009 |
Acta Cryst. (2009). F65, 895-897 [ doi:10.1107/S1744309109029303 ] Crystallization and preliminary structural studies of champedak galactose-binding lectinM. Gabrielsen, A. Riboldi-Tunnicliffe, P. S. Abdul-Rahman, E. Mohamed, W. I. W. Ibrahim, O. H. Hashim, N. W. Isaacs and R. J. CogdellSynopsis: Galactose-binding lectin from champedak was crystallized at 293 K. Preliminary X-ray diffraction analyses are reported. Online 22 August 2009 |
Acta Cryst. (2009). F65, 898-901 [ doi:10.1107/S1744309109028681 ] Overexpression, purification and preliminary X-ray diffraction analysis of the controller protein C.Csp231I from Citrobacter sp. RFL231S. D. Streeter, J. E. McGeehan and G. G. KnealeSynopsis: The crystallization of a novel controller protein is reported and its interaction with DNA is characterized. Online 22 August 2009 |
Acta Cryst. (2009). F65, 902-905 [ doi:10.1107/S1744309109029844 ] Expression, purification, crystallization and preliminary crystallographic analysis of an endo-1,5-
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Acta Cryst. (2009). F65, 906-909 [ doi:10.1107/S174430910903036X ] Expression, purification and preliminary X-ray analysis of proliferating cell nuclear antigen from the archaeon Thermococcus thioreducensM. L. Byrne-Steele and J. D. NgSynopsis: The proliferating cell nuclear antigen (PCNA) from a novel hyperthermophilic archaeon Thermococcus thioreducens has been crystallized, and diffraction data have been collected to 1.86 Å. Online 22 August 2009 |
Acta Cryst. (2009). F65, 910-912 [ doi:10.1107/S1744309109030565 ] Cloning, expression, purification, crystallization and preliminary X-ray analysis of Mycoplasma genitalium protein MG289K. H. Sippel, S. K. Boehlein, Y. Sakai, J. G. Quirit, M. Agbandje-McKenna, C. J. Rosser and R. McKennaSynopsis: Single orthorhombic crystals of M. genitalium protein MG289 have been grown and shown to diffract X-rays to 2.8 Å resolution with good statistics. The structure obtained from these data will help to provide insight into the function of the protein as well as improving the understanding of its role in this human pathogen. Online 22 August 2009 |
Acta Cryst. (2009). F65, 913-916 [ doi:10.1107/S1744309109029881 ] Crystallization and preliminary crystallographic analysis of poly-
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Acta Cryst. (2009). F65, 917-919 [ doi:10.1107/S1744309109031133 ] Crystallization and preliminary X-ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp. BSAR-1K. S. Nilgiriwala, S. C. Bihani, A. Das, V. Prashar, M. Kumar, J.-L. Ferrer, S. K. Apte and M. V. HosurSynopsis: A new alkaline phosphatase enzyme from Sphingomonas sp. strain BSAR-1, termed PhoK, has been shown to be useful in uranium bioprecipitation. PhoK has been expressed, purified and crystallized. Online 22 August 2009 |
Acta Cryst. (2009). F65, 920-922 [ doi:10.1107/S1744309109031261 ] Purification, crystallization and preliminary crystallographic analysis of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris HildenboroughM. Marques, R. Coelho, I. A. C. Pereira and P. M. MatiasSynopsis: Crystals of the soluble form of the [NiFeSe] hydrogenase from D. vulgaris Hildenborough were obtained and belonged to the monoclinic space group P21, with unit-cell parameters a = 60.57, b = 91.05, c = 66.85 Å, Online 22 August 2009 |
Acta Cryst. (2009). F65, 923-925 [ doi:10.1107/S1744309109031248 ] Crystallization and preliminary X-ray analysis of flap endonuclease 1 (FEN1) from Desulfurococcus amylolyticusT. Mase, K. Kubota, K. Miyazono, Y. Kawarabayasi and M. TanokuraSynopsis: Flap endonuclease 1 from D. amylolyticus was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 2.00 Å resolution. Online 22 August 2009 |
Acta Cryst. (2009). F65, 926-929 [ doi:10.1107/S1744309109029157 ] Cobalt-, zinc- and iron-bound forms of adenylate kinase (AK) from the sulfate-reducing bacterium Desulfovibrio gigas: purification, crystallization and preliminary X-ray diffraction analysisA. V. Kladova, O. Y. Gavel, A. Mukhopaadhyay, D. R. Boer, S. Teixeira, V. L. Shnyrov, I. Moura, J. J. G. Moura, M. J. Romão, J. Trincão and S. A. BursakovSynopsis: Adenylate kinase (AK) from D. gigas was purified and crystallized in three different metal-bound forms: Zn2+-AK, Co2+-AK and Fe2+-AK. Online 22 August 2009 |
Acta Cryst. (2009). F65, 930-932 [ doi:10.1107/S1744309109031376 ] Crystallization and preliminary X-ray diffraction studies of the ubiquitin-like (UbL) domain of the human homologue A of Rad23 (hHR23A) proteinY. W. Chen, T. Tajima, M. Rees and M. Garcia-MayaSynopsis: The ubiquitin-like domain of human hHR23A protein was crystallized by the hanging-drop vapour-diffusion method in space group P6522 and diffraction data were collected to 1.97 Å resolution. Structure solution by molecular replacement is described. Online 26 August 2009 |
Acta Cryst. (2009). F65, 933-936 [ doi:10.1107/S1744309109031959 ] Crystallization and preliminary X-ray analysis of aspartate transcarbamoylase from the parasitic protist Trypanosoma cruziK. Matoba, T. Nara, T. Aoki, T. Honma, A. Tanaka, M. Inoue, S. Matsuoka, D. K. Inaoka, K. Kita and S. HaradaSynopsis: Aspartate transcarbamoylase, the second enzyme of the de novo pyrimidine-biosynthetic pathway, from T. cruzi has been purified and crystallized for X-ray structure analysis. Online 26 August 2009 |
Acta Cryst. (2009). F65, 937-940 [ doi:10.1107/S174430910903214X ] Cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of glyceraldehyde-3-phosphate dehydrogenase from Antheraea mylittaS. Mukherjee, S. Maity, S. Roy, S. Ghorai, M. Chakrabarti, R. Agarwal, D. Dutta, A. K. Ghosh and A. K. DasSynopsis: The cloning, overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of glyceraldehyde-3-phosphate dehydrogenase from A. mylitta are reported. Online 26 August 2009 |
Acta Cryst. (2009). F65, 941-944 [ doi:10.1107/S1744309109031352 ] Crystallization of mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanilA. Osanai, S. Harada, K. Sakamoto, H. Shimizu, D. K. Inaoka and K. KitaSynopsis: Rhodoquinol-fumarate reductase is a key enzyme in the anaerobic respiratory chain of adult A. suum mitochondria. Its crystallization in the presence of a mixture of octaethyleneglycol monododecyl ether and n-dodecyl- Online 26 August 2009 |
Acta Cryst. (2009). F65, 945-948 [ doi:10.1107/S1744309109024932 ] Crystallization and preliminary X-ray analysis of the complexes between a Fab and two forms of human insulin-like growth factor IIJ. Newman, E. H. Cohen, L. Cosgrove, K. Kopacz, D. T. Dransfield, T. E. Adams and T. S. PeatSynopsis: Complexes of both hIGF-II and hIGF-IIE with a Fab have been crystallized and investigated by X-ray analysis. Online 26 August 2009 |
Acta Cryst. (2009). F65, 949-951 [ doi:10.1107/S1744309109031662 ] Purification, crystallization and preliminary X-ray analysis of urease from jack bean (Canavalia ensiformis)A. Balasubramanian and K. PonnurajSynopsis: Jack bean urease was purified and crystallized and X-ray diffraction data were collected to 2.05 Å resolution. Online 26 August 2009 |
Acta Cryst. (2009). F65, 952-955 [ doi:10.1107/S1744309109031467 ] Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of leucine aminopeptidase (LAP) from the pepA gene of Xanthomonas oryzae pv. oryzaeK.-H. Huynh, S. Natarajan, J. Choi, N.-H. Song, J.-G. Kim, B.-M. Lee, Y.-J. Ahn and L.-W. KangSynopsis: Leucine aminopeptidase, an exopeptidase that hydrolyzes leucine from the N-terminus of polypeptides, from X. oryzae pv. oryzae was cloned, expressed and crystallized. Online 26 August 2009 |
Acta Cryst. (2009). F65, 956-958 [ doi:10.1107/S1744309109031844 ] Crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of the human spliceosomal DExD/H-box protein hPrp22D. Kudlinzki, C. Nagel and R. FicnerSynopsis: The cloning, purification and crystallization of the C-terminal domain of human hPrp22 are reported. This communication also contains data for the preliminary X-ray diffraction analysis. Online 26 August 2009 |
Acta Cryst. (2009). F65, 959-961 [ doi:10.1107/S1744309109032163 ] Purification, crystallization and initial X-ray diffraction study of the zinc-finger domain of zebrafish NanosH. Hashimoto, S. Kawaguchi, K. Hara, K. Nakamura, T. Shimizu, Y. Tamaru and M. SatoSynopsis: Crystallization of Nanos. Online 26 August 2009 |
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