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Cover illustration: 6-pyruvoyltetrahydropterin synthase homolog SCO 6650 from Streptomyces coelicolor (Spoonamore et al., p. 875). |
Acta Cryst. (2008). F64, 875-879 [ doi:10.1107/S1744309108027048 ] Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolorJ. E. Spoonamore, S. A. Roberts, A. Heroux and V. BandarianSynopsis: The X-ray crystal structure of a 6-pyruvoyltetrahydropterin synthase homolog of unknown function has been determined at 1.5 Å resolution. The protein retains residues required for pterin binding, but nearly all catalytic residues are missing. PDB reference: 3d7j Online 30 September 2008 |
Acta Cryst. (2008). F64, 880-885 [ doi:10.1107/S1744309108028248 ] There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallizationD. Veesler, S. Blangy, C. Cambillau and G. SciaraSynopsis: Crystals of an E. coli AcrB contaminant were grown from 95% pure CorA preparations. This very frequently occurring problem in membrane-protein crystallography laboratories is reported, as well as suggestions to avoid it. PDB reference: 3d9b Online 30 September 2008 |
Acta Cryst. (2008). F64, 886-892 [ doi:10.1107/S1744309108028546 ] Structure and lability of archaeal dehydroquinaseN. N. Smith and D. T. GallagherSynopsis: The structure and thermal melting data for dehydroquinase from A. fulgidus are reported. The protein melts in vitro well below the organism's growth temperature. PDB reference: 2ox1 Online 30 September 2008 |
Acta Cryst. (2008). F64, 893-898 [ doi:10.1107/S1744309108029102 ] Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracisS. Lu, C. D. Smith, Z. Yang, P. S. Pruett, L. Nagy, D. McCombs, L. J. DeLucas, W. J. Brouillette and C. G. BrouilletteSynopsis: The crystal structure of apo nicotinic acid mononucleotide adenylyltransferase (NaMNAT) from B. anthracis was determined to 2.3 Å resolution and compared with other bacterial NaMNAT structures. PDB reference: 3dv2 Online 30 September 2008 |
Acta Cryst. (2008). F64, 899-902 [ doi:10.1107/S1744309108026791 ] Crystallization and preliminary X-ray analysis of the Thermoplasma acidophilum 20S proteasome in complex with protein substratesK. Felderer, M. Groves, J. Diez, E. Pohl and S. WittSynopsis: Host-guest complexes of 20S proteasomes with either cytochrome c (cyt c) or green fluorescent protein (GFP) trapped inside the inner cavities of the proteasome have been crystallized. Diffraction data were collected to 3.4 Å (cyt c) and 3.8 Å (GFP) resolution using a synchrotron-radiation source. Online 30 September 2008 |
Acta Cryst. (2008). F64, 903-910 [ doi:10.1107/S1744309108026924 ] Crystallization and preliminary crystallographic studies of putative threonyl-tRNA synthetases from Aeropyrum pernix and Sulfolobus tokodaiiS. Shimizu, E. C. M. Juan, Y. Miyashita, Y. Sato, M. M. Hoque, K. Suzuki, M. Yogiashi, M. Tsunoda, A.-C. Dock-Bregeon, D. Moras, T. Sekiguchi and A. TakénakaSynopsis: Two types of putative threonyl-tRNA synthetases with complementary functions from the crenarchaea A. pernix K1 and S. tokodaii strain 7 have been overexpressed, purified and crystallized. The crystal structure of one of the four proteins, the catalytic type ThrRS from A. pernix, has successfully been solved by the Se-MAD method. Online 30 September 2008 |
Acta Cryst. (2008). F64, 911-913 [ doi:10.1107/S1744309108026869 ] Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP)S. Terawaki, K. Kitano, M. Aoyama and T. HakoshimaSynopsis: The radixin FERM domain was shown to bind the MT1-MMP cytoplasmic peptide and crystals of the complex were obtained. Online 30 September 2008 |
Acta Cryst. (2008). F64, 914-917 [ doi:10.1107/S1744309108026870 ] Purification, crystallization and preliminary crystallographic studies of SPCI-chymotrypsin complex at 2.8 Å resolutionA. J. da Silva, R. C. L. Teles, G. F. Esteves, C. R. dos Santos, J. A. R. G. Barbosa and S. M. de FreitasSynopsis: S. parahyba chymotrypsin inhibitor in complex with chymotrypsin has been purified and crystallized using the vapour-diffusion method and preliminarily analysis has been performed using X-ray diffraction. Online 30 September 2008 |
Acta Cryst. (2008). F64, 918-921 [ doi:10.1107/S1744309108027036 ] Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venomD. Georgieva, A. Kardas, F. Buck, M. Perbandt and C. BetzelSynopsis: A novel L-amino-acid oxidase was isolated from V. ammodytes ammodytes venom and crystallized. The solution conditions under which the protein sample was monodisperse were optimized using dynamic light scattering prior to crystallization. Preliminary diffraction data were collected to 2.6 Å resolution. Online 30 September 2008 |
Acta Cryst. (2008). F64, 922-925 [ doi:10.1107/S1744309108027462 ] Expression, purification, crystallization and preliminary crystallographic study of the SRA domain of the human UHRF1 proteinB. Delagoutte, N. Lallous, C. Birck, P. Oudet and J.-P. SamamaSynopsis: The SET- and RING finger-associated (SRA) domain of human UHRF1 protein has been overexpressed in E. coli, purified and crystallized. The three-dimensional structure of the protein in its SeMet form was solved from 2.2 Å diffraction data using the multiple anomalous dispersion method. Online 30 September 2008 |
Acta Cryst. (2008). F64, 926-928 [ doi:10.1107/S1744309108027516 ] Crystallization and preliminary X-ray diffraction analysis of the HsdR subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016N. T. Uyen, K. Nishi, S.-Y. Park, J.-W. Choi, H.-J. Lee and J.-S. KimSynopsis: The crystallization of the HsdR subunit of a putative type I restriction-modification system from V. vulnificus and the collection of diffraction data to 2.6 Å resolution are reported. Online 30 September 2008 |
Acta Cryst. (2008). F64, 929-932 [ doi:10.1107/S1744309108027504 ] Expression, purification, crystallization and preliminary X-ray diffraction studies of glyceraldehyde-3-phosphate dehydrogenase 1 from methicillin-resistant Staphylococcus aureus (MRSA252)S. Mukherjee, D. Dutta, B. Saha and A. K. DasSynopsis: The cloning, overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from MRSA252 are reported. Online 30 September 2008 |
Acta Cryst. (2008). F64, 933-935 [ doi:10.1107/S1744309108027796 ] Expression, purification, crystallization and preliminary X-ray analysis of an archaeal protein homologous to plant nicotianamine synthaseC. Dreyfus, D. Pignol and P. ArnouxSynopsis: A putative nicotianamine synthase from M. thermoautotrophicus was cloned, expressed, purified and crystallized. The native crystals diffracted to a resolution of 1.7 Å. Online 30 September 2008 |
Acta Cryst. (2008). F64, 936-941 [ doi:10.1107/S1744309108027930 ] Purification, crystallization and preliminary X-ray diffraction analysis of the CBS-domain pair from the Methanococcus jannaschii protein MJ0100M. Lucas, D. Kortazar, E. Astigarraga, J. A. Fernández, J. M. Mato, M. L. Martínez-Chantar and L. A. Martínez-CruzSynopsis: The C-terminal domain of the Methanococcus jannaschii protein MJ0100 includes a CBS-domain pair and has been overexpressed, purified and crystallized. Crystals of selenomethionine-substituted (SeMet) protein were also grown. Online 30 September 2008 |
Acta Cryst. (2008). F64, 942-944 [ doi:10.1107/S1744309108028236 ] Crystallization and preliminary X-ray diffraction studies of an RNA aptamer in complex with the human IgG Fc fragmentS. Sugiyama, Y. Nomura, T. Sakamoto, T. Kitatani, A. Kobayashi, S. Miyakawa, Y. Takahashi, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, Y. Nakamura and H. MatsumuraSynopsis: An RNA aptamer in complex with the human IgG Fc fragment have been crystallized. The stirring technique with a rotary shaker was used to improve the crystals and to ensure that they were of high quality and single, resulting in crystals that diffracted to 2.2 Å resolution. Online 30 September 2008 |
Acta Cryst. (2008). F64, 945-948 [ doi:10.1107/S1744309108028352 ] Overexpression, purification, crystallization and preliminary X-ray crystal analysis of Bacillus pallidus D-arabinose isomeraseK. Takeda, H. Yoshida, G. Takada, K. Izumori and S. KamitoriSynopsis: Recombinant B. pallidus D-arabinose isomerase was crystallized and diffraction data were collected to 2.3 Å resolution. Online 30 September 2008 |
Acta Cryst. (2008). F64, 949-953 [ doi:10.1107/S174430910802842X ] Three crystal forms of the bifunctional enzyme proline utilization A (PutA) from Bradyrhizobium japonicumJ. P. Schuermann, T. A. White, D. Srivastava, D. B. Karr and J. J. TannerSynopsis: The first diffraction-quality crystals of a PutA protein are reported. One of the three crystal forms described here exhibits pseudo-merohedral twinning. Removal of the N-terminal histidine tag aided the crystallization of another form. Online 30 September 2008 |
Acta Cryst. (2008). F64, 954-956 [ doi:10.1107/S1744309108028522 ] Initial crystallographic study of human PCNA in complex with a peptide containing the noncanonical PIP-box sequence of human DNA polymerase
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Acta Cryst. (2008). F64, 957-959 [ doi:10.1107/S1744309108028571 ] Crystallization and preliminary X-ray study of alkaline
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Acta Cryst. (2008). F64, 960-965 [ doi:10.1107/S1744309108028704 ] Effect of leucine-to-methionine substitutions on the diffraction quality of histone chaperone SET/TAF-I
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Acta Cryst. (2008). F64, 966-969 [ doi:10.1107/S1744309108029515 ] Overproduction, purification and preliminary X-ray diffraction analysis of YncE, an iron-regulated Sec-dependent periplasmic protein from Escherichia coliA. Baba-Dikwa, D. Thompson, N. J. Spencer, S. C. Andrews and K. A. WatsonSynopsis: The YncE protein of E. coli has been overproduced and purified and preliminary crystallographic analysis has been performed to 2.1 Å resolution. The structure reveals a seven-bladed Online 30 September 2008 |
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