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Cover illustration: Mouse ADP-ribosylhydrolase 3. Ribbon-plot representation and protein solvent-accessible surface representation. The colouring scheme for the protein chain is from the N-terminus (blue) to the C-terminus (red). The solvent-accessible surface is coloured grey and the two Mg2+ ions are shown as cyan spheres (Mueller-Dieckmann, Kernstock, Mueller-Dieckmann, Weiss & Koch-Nolte, p. 156). |
Acta Cryst. (2008). F64, 154-155 [ doi:10.1107/S1744309108005617 ]
Online 29 February 2008
![]() | Acta Cryst. (2008). F64, 156-162 [ doi:10.1107/S1744309108001413 ] Structure of mouse ADP-ribosylhydrolase 3 (mARH3)C. Mueller-Dieckmann, S. Kernstock, J. Mueller-Dieckmann, M. S. Weiss and F. Koch-NolteSynopsis: The crystal structure of ADP-ribosylhydrolase 3 from M. musculus has been determined and refined to a resolution of 1.8 Å. A detailed comparison with the human orthologue at the protein-sequence level as well as of the three-dimensional architecture is presented. PDB reference: 2qty Online 23 February 2008 |
Acta Cryst. (2008). F64, 163-166 [ doi:10.1107/S1744309108002078 ] A novel acetate-bound complex of human carbonic anhydrase IIP. A. Mazumdar, D. Kumaran, S. Swaminathan and A. K. DasSynopsis: A complex of human carbonic anhydrase II with its inhibitor acetate is described where the ligand is found to bind in an orientation different from that previously described. PDB reference: 1xeg Online 23 February 2008 |
Acta Cryst. (2008). F64, 167-170 [ doi:10.1107/S1744309108002753 ] Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosisR. Vyas, V. Kumar, S. Panjikar, S. Karthikeyan, K. V. R. Kishan, R. Tewari and M. S. WeissSynopsis: The enzyme aspartate semialdehyde dehydrogenase from M. tuberculosis has been expressed, purified and crystallized in two different crystal forms. Online 23 February 2008 |
Acta Cryst. (2008). F64, 171-174 [ doi:10.1107/S1744309108002662 ] Preparation, crystallization and preliminary X-ray diffraction analysis of the DNA-binding domain of the Ets transcription factor in complex with target DNAY. Suwa, T. Nakamura, S. Toma, S. Ikemizu, H. Kai and Y. YamagataSynopsis: The complex between the Ets domain of Ets2 and its target DNA has been crystallized. The crystals diffracted to 3.0 Å resolution. Online 23 February 2008 |
Acta Cryst. (2008). F64, 175-178 [ doi:10.1107/S1744309108003370 ] Crystallization and preliminary X-ray analysis of human Brn-5 transcription factor in complex with DNAJ. H. Pereira, S. C. Ha and S.-H. KimSynopsis: The human Brn-5 transcription factor has been crystallized in complex with DNA. Diffraction data were collected to 2.80 Å. Online 23 February 2008 |
Acta Cryst. (2008). F64, 179-181 [ doi:10.1107/S1744309108003473 ] Crystallization and preliminary X-ray diffraction analysis of full-length and proteolytically activated pyruvate oxidase from Escherichia coliA. Weidner, P. Neumann, G. Wille, M. T. Stubbs and K. TittmannSynopsis: The peripheral membrane flavoprotein pyruvate oxidase from E. coli has been crystallized in the full-length form and as a proteolytically activated truncation variant lacking the last 23 amino acids at the C-terminus. Online 23 February 2008 |
Acta Cryst. (2008). F64, 182-185 [ doi:10.1107/S174430910800345X ] Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus nigerK. E. Atkin, R. Reiss, N. J. Turner, A. M. Brzozowski and G. GroganSynopsis: Crystals of A. niger monoamine oxidase variants display P21 or P41212/P43212 symmetry, with eight or two molecules in the asymmetric unit, respectively. Online 23 February 2008 |
Acta Cryst. (2008). F64, 186-189 [ doi:10.1107/S1744309108003667 ] Crystallization and preliminary X-ray studies of ferredoxin-NAD(P)+ reductase from Chlorobium tepidumN. Muraki, D. Seo, T. Shiba, T. Sakurai and G. KurisuSynopsis: Ferredoxin-NAD(P)+ reductase from C. tepidum has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.4 Å resolution. Online 23 February 2008 |
Acta Cryst. (2008). F64, 190-192 [ doi:10.1107/S1744309108003680 ]
Synopsis: A catalytically inactive mutant of the dual-specificity phosphatase H1L from vaccinia virus was expressed recombinantly, purified and crystallized by the microbatch method. The crystals belong to the tetragonal space group P422 and diffraction data were collected to 2.1 Å resolution using a synchrotron-radiation source. Attempts to derivatize these crystals with xenon gas lead to a space-group change to I422 with a smaller unit cell and a diffraction limit of 3.0 Å.
Online 23 February 2008
Acta Cryst. (2008). F64, 193-195 [ doi:10.1107/S1744309108003825 ] Crystallization and preliminary X-ray crystallographic characterization of TrmFO, a folate-dependent tRNA methyltransferase from Thermotoga maritimaN. CicmilSynopsis: T. maritima TrmFO was overexpressed, purified and crystallized. A diffraction data set was collected to a resolution of 2.6 Å. Online 23 February 2008 |
Acta Cryst. (2008). F64, 196-199 [ doi:10.1107/S1744309108003849 ] Crystallization and preliminary X-ray analysis of RsbS from Moorella thermoacetica at 2.5 Å resolutionM. Quin, J. Newman, S. Firbank, R. J. Lewis and J. Marles-WrightSynopsis: Crystallization and selenium substructure solution of RsbS from Moorella thermoacetica, the first ab initio phased crystal structure from Diamond. Online 23 February 2008 |
Acta Cryst. (2008). F64, 200-202 [ doi:10.1107/S1744309107068388 ] Expression, purification, crystallization and preliminary X-ray diffraction analysis of grass carp
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Acta Cryst. (2008). F64, 203-205 [ doi:10.1107/S1744309108002510 ] Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6A. Tsalafouta, E. Psylinakis, E. G. Kapetaniou, D. Kotsifaki, A. Deli, A. Roidis, V. Bouriotis and M. KokkinidisSynopsis: The peptidoglycan N-acetylglucosamine (GlcNAc) deacetylase BC1960 from B. cereus was crystallized in the presence of the substrate (GlcNAc)6. The crystals belonged to space group P41212 and diffracted to 2.38 Å resolution. Online 29 February 2008 |
Acta Cryst. (2008). F64, 206-208 [ doi:10.1107/S1744309108002819 ] The purification, crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Clostridium botulinumR. C. J. Dobson, S. C. Atkinson, M. A. Gorman, J. M. Newman, M. W. Parker and M. A. PeruginiSynopsis: Dihydrodipicolinate synthase (DHDPS), an enzyme in the lysine-biosynthetic pathway, is a promising target for antibiotic development against pathogenic bacteria. Here, the expression, purification, crystallization and preliminary diffraction analysis of DHDPS from C. botulinum are reported. Online 29 February 2008 |
Acta Cryst. (2008). F64, 209-212 [ doi:10.1107/S1744309108002832 ] Crystallization and preliminary X-ray study of native and selenomethionyl
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Acta Cryst. (2008). F64, 213-216 [ doi:10.1107/S1744309108003096 ] Expression, purification, crystallization and preliminary X-ray characterization of two crystal forms of stationary-phase survival E protein from Campylobacter jejuniA. M. D. Gonçalves, A. T. Rêgo, M. Thomaz, F. J. Enguita and M. A. CarrondoSynopsis: Survival E (SurE) protein from Campylobacter jejuni, a Gram-negative mesophile, has been overexpressed in Escherichia coli as a soluble protein, successfully purified and crystallized in two distinct crystal forms. Online 29 February 2008 |
Acta Cryst. (2008). F64, 217-220 [ doi:10.1107/S1744309108003795 ] Crystallization and preliminary X-ray diffraction studies of polyketide synthase-1 (PKS-1) from Cannabis sativaC. Taguchi, F. Taura, T. Tamada, Y. Shoyama, Y. Shoyama, H. Tanaka, R. Kuroki and S. MorimotoSynopsis: Polyketide synthase-1 from C. sativa has been crystallized. The crystal diffracted to 1.55 Å resolution with sufficient quality for further structure determination. Online 29 February 2008 |
Acta Cryst. (2008). F64, 221-223 [ doi:10.1107/S1744309108004211 ] Overproduction, purification and crystallization of a chondroitin sulfate A-binding DBL domain from a Plasmodium falciparum var2csa-encoded PfEMP1 proteinM. K. HigginsSynopsis: A chondroitin sulfate A-binding DBL important in placental malaria has been overproduced, purified and crystallized. Diffraction data were collected to 1.9 Å resolution. Online 29 February 2008 |
Acta Cryst. (2008). F64, 224-227 [ doi:10.1107/S1744309108004387 ] Expression, purification, crystallization and preliminary X-ray analysis of the polysaccharide lyase RB5312 from the marine planctomycete Rhodopirellula balticaJ. Dabin, M. Jam, M. Czjzek and G. MichelSynopsis: This study describes the crystallization and preliminary X-ray analysis of the family PL1 polysaccharide lyase RB5312 from the marine bacterium R. baltica. Purified recombinant protein was crystallized; the crystals belonged to space group P212121 and diffracted X-rays to a resolution of 1.8 Å. Online 29 February 2008 |
Acta Cryst. (2008). F64, 228-230 [ doi:10.1107/S1744309108004326 ] Crystallization and preliminary X-ray crystallographic analysis of rabbit L-gulonate 3-dehydrogenaseY. Asada, C. Kuroishi, Y. Ukita, R. Sumii, S. Endo, T. Matsunaga, A. Hara and N. KunishimaSynopsis: The preliminary X-ray crystallographic study of rabbit L-gulonate 3-dehydrogenase is described. Online 29 February 2008 |
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