![]() ![]() |
|
![]() |
Cover illustration: A selection of the best crystal pictures published in Acta Cryst. F in 2010. |
Acta Cryst. (2011). F67, 1 [ doi:10.1107/S1744309110053959 ] EditorialH. Einspahr and M. S. WeissSynopsis: Editorial. Online 24 December 2010 |
Acta Cryst. (2011). F67, 2-16 [ doi:10.1107/S1744309110035037 ] Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organismsS. P. Kanaujia, J. Jeyakanthan, A. Shinkai, S. Kuramitsu, S. Yokoyama and K. SekarSynopsis: Three crystal structures of the molybdenum-cofactor biosynthesis protein MogA from two highly thermophilic organisms have been determined at high resolution. Comparative analyses revealed the residues involved in oligomerization. In addition, molecular-dynamics and docking studies suggested the binding affinities of several small molecules towards MogA and homologous proteins. PDB references: 3mch, 3mci and 3mcj Online 21 December 2010 |
Acta Cryst. (2011). F67, 17-22 [ doi:10.1107/S1744309110043113 ] Structures of the SEp22 dodecamer, a Dps-like protein from Salmonella enterica subsp. enterica serovar EnteritidisT. Miyamoto, Y. Asahina, S. Miyazaki, H. Shimizu, U. Ohto, S. Noguchi and Y. SatowSynopsis: The crystal structure of SEp22, a DNA-binding protein from starved cells from S. enterica subsp. enterica serovar Enteritidis, was determined in two forms: the native state at 1.25 Å resolution and an iron-soaked form at 1.30 Å resolution. Online 21 December 2010 |
Acta Cryst. (2011). F67, 23-26 [ doi:10.1107/S174430911004443X ] Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutansÅ. Nylander, N. Forsgren and K. PerssonSynopsis: The structure of the C-terminal domain of the S. mutans surface adhesin SpaP has been determined to 2.2 Å resolution. PDB reference: 3opu Online 21 December 2010 |
Acta Cryst. (2011). F67, 27-32 [ doi:10.1107/S1744309110046099 ] Structure of laccase from Streptomyces coelicolor after soaking with potassium hexacyanoferrate and at an improved resolution of 2.3 ÅT. Skálová, J. Dusková, J. Hasek, A. Stepánková, T. Koval, L. H. Østergaard and J. DohnálekSynopsis: The structure of the small laccase from S. coelicolor is reported at improved resolution and in a different space group. The soaked ligand is bound between laccase molecules. PDB reference: 3kw8 Online 21 December 2010 |
Acta Cryst. (2011). F67, 33-37 [ doi:10.1107/S174430911004724X ] Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active siteK. L. Barrack, L. B. Tulloch, L.-A. Burke, P. K. Fyfe and W. N. HunterSynopsis: The structure of L. donovani pteridine reductase has been targeted to assist in a program of structure-based inhibitor research. Crystals that diffracted to 2.5 Å resolution were obtained and the structure has been solved. Unfortunately, the active site is disordered and this crystal form is unsuitable for use in characterizing enzyme-ligand interactions. PDB reference: 2xox Online 21 December 2010 |
Acta Cryst. (2011). F67, 38-40 [ doi:10.1107/S1744309110041011 ] Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferaseG. B. Kang, M.-K. Kim, H.-S. Youn, J. Y. An, J.-G. Lee, K. R. Park, S. H. Lee, Y. Kim, S.-I. Fukuoka and S. H. EomSynopsis: H. sapiens quinolinate phosphoribosyltransferase has been expressed, purified and crystallized. A diffraction data set has been collected and processed at 2.8 Å resolution. Online 21 December 2010 |
Acta Cryst. (2011). F67, 41-43 [ doi:10.1107/S1744309110036432 ] Crystallization and preliminary X-ray studies of native and mutant intimin from enterohaemorrhagic Escherichia coliY. Yi, F. Gao, X. Mao, M. Xiao, P. Luo, J. Qi, G. Guo, H. Jing, Y. Cui and Q. ZouSynopsis: Crystals of native intimin and its N916Y mutant from enterohaemorrhagic E. coli O157:H7 diffracted to 2.8 and 2.6 Å resolution, respectively. Online 21 December 2010 |
Acta Cryst. (2011). F67, 44-47 [ doi:10.1107/S1744309110038820 ] Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of the co-chaperonin XoGroES from Xanthomonas oryzae pv. oryzaeT. T. N. Doan, S. Natarajan, N.-H. Song, J. Kim, J.-K. Kim, S. Kim, P. T. Viet, J.-G. Kim, B.-M. Lee, Y.-J. Ahn and L.-W. KangSynopsis: Bacterial blight, an infectious disease caused by X. oryzae pv. oryzae (Xoo), causes huge rice-production losses in most rice-cultivating countries. The co-chaperonin of Xoo, XoGroES, an important protein for protein folding, was cloned from Xoo, purified and crystallized for atomic resolution structure determination. Online 21 December 2010 |
Acta Cryst. (2011). F67, 48-50 [ doi:10.1107/S1744309110042156 ] Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domainT. Vognsen, I. R. Möller and O. KristensenSynopsis: The human G3BP1 NTF2-like domain was crystallized. Diffraction data were collected to 3.6 Å resolution. Online 21 December 2010 |
Acta Cryst. (2011). F67, 51-53 [ doi:10.1107/S1744309110043174 ] Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureusA. Begum, J. Drebes, M. Perbandt, C. Wrenger and C. BetzelSynopsis: Crystals of the thiaminase type II from S. aureus are orthorhombic, belonging to space group P212121 with unit-cell parameters a = 103.5, b = 104.1, c = 109.6 Å, and diffracted to 2.6 Å resolution. Online 21 December 2010 |
Acta Cryst. (2011). F67, 54-58 [ doi:10.1107/S1744309110043472 ] Crystallization and preliminary crystallographic characterization of three peptidic inhibitors in complex with
|
Acta Cryst. (2011). F67, 59-63 [ doi:10.1107/S1744309110043393 ] Anaerobic crystallization and initial X-ray diffraction data of biphenyl 2,3-dioxygenase from Burkholderia xenovorans LB400: addition of agarose improved the quality of the crystalsP. Kumar, L. Gómez-Gil, M. Mohammadi, M. Sylvestre, L. D. Eltis and J. T. BolinSynopsis: Biphenyl 2,3-dioxygenase from B. xenovorans LB400 and its variants BPDOP4 and BPDORR41 were crystallized using agarose gel and the crystals were characterized using X-ray diffraction. Online 21 December 2010 |
Acta Cryst. (2011). F67, 64-67 [ doi:10.1107/S1744309110043770 ] Crystallization and preliminary X-ray analysis of the vWA domain of human anthrax toxin receptor 1C. Cai, Y. Zhao, X. Tong, S. Fu, Y. Li, Y. Wu, X. Li and Z. LouSynopsis: The vWA domain of human anthrax toxin receptor 1 was overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 1.8 Å resolution. Online 22 December 2010 |
Acta Cryst. (2011). F67, 68-71 [ doi:10.1107/S1744309110043721 ] Crystallization and preliminary crystallographic analysis of the glycoside hydrolase family 115
|
Acta Cryst. (2011). F67, 72-75 [ doi:10.1107/S1744309110044465 ] Expression, purification, crystallization and preliminary X-ray analysis of wild-type and of an active-site mutant of glyceraldehyde-3-phosphate dehydrogenase from Campylobacter jejuniD. S. Tourigny, P. R. Elliott, L. J. Edgell, G. M. Hudson and P. C. E. MoodySynopsis: The cloning, expression, purification, crystallization and preliminary X-ray analysis of wild-type and of an active-site mutant of C. jejuni glyceraldehyde-3-phosphate dehydrogenase is reported. Online 22 December 2010 |
Acta Cryst. (2011). F67, 76-78 [ doi:10.1107/S174430911004457X ] Purification, crystallization and preliminary crystallographic analysis of SMU.1108c protein from Streptococcus mutansM.-J. Feng, T.-M. Fu, X. Liu and L.-F. LiSynopsis: SMU.1108c, a putative uncharacterized protein from S. mutans, was crystallized and X-ray diffraction data were collected to a resolution of 2.2 Å. Online 22 December 2010 |
Acta Cryst. (2011). F67, 79-82 [ doi:10.1107/S1744309110045616 ] Purification and crystallization of RNase HIII from Staphylococcus aureusS. A. Reiling, K. Homma and O. A. AsojoSynopsis: The purification, crystallization and preliminary X-ray diffraction analysis of RNase HIII from S. aureus is presented. Crystals that diffracted to 2.6 Å resolution in space group P212121 were only obtained after removal of the hexahistidine tag. Online 22 December 2010 |
Acta Cryst. (2011). F67, 83-86 [ doi:10.1107/S174430911004618X ] Cloning, purification, crystallization and preliminary X-ray analysis of ESX-1-secreted protein regulator (EspR) from Mycobacterium tuberculosisS. P. Gangwar, S. R. Meena and A. K. SaxenaSynopsis: ESX-1 secreted protein regulator (EspR, Rv3849) from M. tuberculosis has been purified and crystallized, and diffracted to 3.2 Å resolution at wavelength 0.97625 Å. Online 23 December 2010 |
Acta Cryst. (2011). F67, 87-89 [ doi:10.1107/S1744309110046178 ] Purification, crystallization and X-ray diffraction study of basic 7S globulin from soybeanT. Yoshizawa, H. Hashimoto, T. Shimizu, M. Yamabe, N. Shichijo, K. Hanada, H. Hirano and M. SatoSynopsis: Crystallization of basic 7S globulin from soybean is presented. Online 23 December 2010 |
Acta Cryst. (2011). F67, 90-93 [ doi:10.1107/S1744309110046208 ] Crystallization of an apo form of human arginase: using all the tools in the toolbox simultaneouslyJ. Newman, L. Pearce, C. A. Lesburg, C. Strickland and T. S. PeatSynopsis: An apo form of human arginase I which is suitable for soaking experiments has been crystallized. Online 23 December 2010 |
Acta Cryst. (2011). F67, 94-97 [ doi:10.1107/S1744309110046580 ] Crystallization and preliminary X-ray crystallographic analysis of the NmrA-like DDB_G0286605 protein from the social amoeba Dictyostelium discoideumM.-K. Kim, H.-S. Yim and S.-O. KangSynopsis: In order to investigate its structure and function, the NmrA-like domain-containing DDB_G0286605 protein from D. discoideum was expressed, purified and crystallized. X-ray diffraction analysis is reported to a resolution of 1.64 Å. Online 23 December 2010 |
Acta Cryst. (2011). F67, 98-100 [ doi:10.1107/S1744309110046932 ] Crystallization and preliminary X-ray crystallographic analysis of the short-chain dehydrogenase/reductase-type DDB_G0291732 protein from Dictyostelium discoideumM.-K. Kim, H.-S. Yim and S.-O. KangSynopsis: In order to investigate its structure and function, the NmrA-like short-chain dehydrogenase/reductase-type DDB_G0291732 protein from D. discoideum was expressed, purified and crystallized. X-ray diffraction analysis is reported to a resolution of 1.65 Å. Online 23 December 2010 |
Acta Cryst. (2011). F67, 101-103 [ doi:10.1107/S1744309110046944 ] Crystallization and preliminary X-ray analysis of isopentenyl diphosphate isomerase from Methanocaldococcus jannaschiiT. Hoshino, E. Nango, S. Baba, T. Eguchi and T. KumasakaSynopsis: Isopentenyl diphosphate isomerase from M. jannaschii has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.08 Å resolution. Online 23 December 2010 |
Acta Cryst. (2011). F67, 104-110 [ doi:10.1107/S174430911004697X ] Crystallization of the nonameric small terminase subunit of bacteriophage P22A. Roy, A. Bhardwaj and G. CingolaniSynopsis: The small terminase subunit of bacteriophage P22 was overexpressed in E. coli, purified under native conditions and crystallized as a nonamer. High-quality diffraction data were collected to 1.75 Å resolution using synchrotron radiation. Online 23 December 2010 |
Acta Cryst. (2011). F67, 111-113 [ doi:10.1107/S1744309110046981 ] Expression, purification and preliminary crystallographic analysis of the recombinant
|
Acta Cryst. (2011). F67, 114-116 [ doi:10.1107/S1744309110047305 ] Crystallization of Escherichia coli maltoporin in the trigonal space group R3M. Blaise and S. ThirupSynopsis: The crystallization of E. coli maltoporin in a new crystal form that diffracts to high resolution is reported. Online 23 December 2010 |
Acta Cryst. (2011). F67, 117-120 [ doi:10.1107/S1744309110047640 ] Cloning, expression, purification and preliminary X-ray analysis of the protein kinase domain of constitutive triple response 1 (CTR1) from Arabidopsis thalianaH. Mayerhofer, C. Mueller-Dieckmann and J. Mueller-DieckmannSynopsis: Wild-type and a kinase-dead mutant of the C-terminal serine/threonine kinase domain of CTR1 from A. thaliana were expressed and crystallized. The crystals belonged to space groups P41212 and P42212, respectively. Online 23 December 2010 |
Acta Cryst. (2011). F67, 121-123 [ doi:10.1107/S1744309110048220 ] Crystallization and preliminary X-ray diffraction analysis of the azoreductase PpAzoR from Pseudomonas putida MET94B. Correia, Z. Chen, S. Mendes, L. O. Martins and I. BentoSynopsis: PpAzoR, an FMN-dependent NADPH azoreductase from Pseudomonas putida MET94, has been crystallized using the sitting-drop vapour-diffusion technique. Online 23 December 2010 |
Acta Cryst. (2011). F67, 124-128 [ doi:10.1107/S1744309110048177 ] Crystallization of recombinant bifunctional nuclease TBN1 from tomatoT. Koval', P. Lipovová, T. Podzimek, J. Matousek, J. Dusková, T. Skálová, A. Stepánková, J. Hasek and J. DohnálekSynopsis: Glycosylated recombinant bifunctional nuclease from tomato has been crystallized and preliminary X-ray diffraction analysis was performed. Online 23 December 2010 |
Acta Cryst. (2011). F67, 129-132 [ doi:10.1107/S1744309110048153 ] Crystallization and preliminary crystallographic analysis of human LR11 Vps10p domainZ. Nakata, M. Nagae, N. Yasui, H. Bujo, T. Nogi and J. TakagiSynopsis: LR11/sorLA contains in its extracellular region a large ( Online 23 December 2010 |
Acta Cryst. (2011). F67, 133-135 [ doi:10.1107/S1744309110048104 ] Cloning, expression, purification, crystallization and preliminary crystallographic analysis of NifH2 from Methanocaldococcus jannaschiiK. Huang, J. Ma, Y. Yuan and Y. GaoSynopsis: NifH2, a homologue of nitrogenase reductase from Methanocaldococcus jannaschii was cloned, overexpressed, purified and crystallized. X-ray diffraction data were collected to 2.85 Å resolution and the crystals belonged to space group P2. Online 23 December 2010 |
Acta Cryst. (2011). F67, 136-139 [ doi:10.1107/S1744309110048268 ] Preliminary X-ray crystallographic analysis of the glycosyltransferase from a marine Streptomyces speciesL. Gong, Y. Xiao, Q. Liu, S. Li, C. Zhang and J. LiuSynopsis: The recombinant glycosyltransferase ElaGT from the elaiophylin-producing marine Streptomyces sp. SCSIO 01934 has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.9 Å resolution. Online 23 December 2010 |
Acta Cryst. (2011). F67, 140-143 [ doi:10.1107/S174430911004844X ] Crystallization and preliminary X-ray diffraction analysis of L,L-diaminopimelate aminotransferase (DapL) from Chlamydomonas reinhardtiiA. O. Hudson, I. Girón and R. C. J. DobsonSynopsis: A variant of the diaminopimelate/lysine pathway has recently been defined following the discovery of the enzyme L,L-diaminopimelate aminotransferase (DapL). The cloning of the cDNA, recombinant expression, purification and preliminary diffraction analysis of DapL from the alga C. reinhardtii are presented. Online 24 December 2010 |
Acta Cryst. (2011). F67, 144-146 [ doi:10.1107/S1744309110048426 ] Expression, purification, crystallization and preliminary X-ray analysis of the KaiC-like protein PH0187 from the hyperthermophilic archaeon Pyrococcus horikoshii OT3H.-J. Kang, K. Kubota, K. Miyazono and M. TanokuraSynopsis: The KaiC-like protein PH0187 from the hyperthermophilic archaeon P. horikoshii OT3 was expressed, purified and crystallized using the sitting-drop vapour-diffusion method. The crystal of PH0187 diffracted X-rays to 2.75 Å resolution. Online 24 December 2010 |
Acta Cryst. (2011). F67, 147-149 [ doi:10.1107/S1744309110048438 ] Crystallization and preliminary crystallographic analysis of D-serine dehydratase from chicken kidneyM. Senda, H. Tanaka, T. Ishida, K. Horiike and T. SendaSynopsis: D-Serine dehydratase purified from chicken kidney was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.09 Å resolution. Online 24 December 2010 |
Acta Cryst. (2011). F67, 150-152 [ doi:10.1107/S1744309110048451 ] Crystallization and preliminary X-ray analysis of a cold-active endo-
|
Acta Cryst. (2011). F67, 153-156 [ doi:10.1107/S1744309110048542 ] Purification, crystallization and preliminary X-ray diffraction analysis of the seryl-tRNA synthetase from Candida albicansR. Rocha, P. J. Barbosa Pereira, M. A. S. Santos and S. Macedo-RibeiroSynopsis: The seryl-tRNA synthetase from C. albicans was crystallized by the sitting-drop vapour-diffusion method using ammonium sulfate as precipitant. The crystals belonged to the hexagonal space group P6122 and diffraction data were collected to 2.0 Å resolution at a synchrotron source. Online 24 December 2010 |
Acta Cryst. (2011). F67, 157-160 [ doi:10.1107/S1744309110048803 ] Expression, purification and crystallization of VP4 protease from Tellina virus 1I. Y. W. Chung and M. PaetzelSynopsis: Limited proteolysis of a monomeric fraction of Tellina virus 1 VP4 protease leads to crystals that diffract to beyond 2.1 Å resolution. Online 24 December 2010 |
Acta Cryst. (2011). F67, 161-163 [ doi:10.1107/S1744309110049171 ] Crystallization and preliminary X-ray diffraction analysis of the lytic transglycosylase MltE from Escherichia coliC. Artola-Recolons, L. I. Llarrull, E. Lastochkin, S. Mobashery and J. A. HermosoSynopsis: Crystals of the lytic transglycosylase MltE from E. coli were grown using the microbatch method and diffracted to a resolution of 2.1 Å. Online 24 December 2010 |
Acta Cryst. (2011). F67, 164-168 [ doi:10.1107/S1744309110049845 ] Expression, purification, crystallization and preliminary X-ray crystallographic analysis of a major fragment of the resuscitation-promoting factor RpfB from Mycobacterium tuberculosisA. Ruggiero, F. Squeglia, L. Pirone, S. Correale and R. BerisioSynopsis: In this study, the region 115-362 of the resuscitation-promoting factor RpfB was cloned, expressed and crystallized. This region includes the C-terminal catalytic domain, the G5 domain and one of the three DUF348 domains, which are of previously unknown structure and function. Online 24 December 2010 |
Acta Cryst. (2011). F67, 169-172 [ doi:10.1107/S1744309110050785 ] The mimivirus R355 gene product: preliminary crystallographic analysis of a putative ubiquitin-like protein-specific proteaseS. Jeudy, A. Lartigue, P. Mansuelle, Y. Ogata and C. AbergelSynopsis: The genome sequence of mimivirus, the largest known double-stranded DNA virus, encodes a putative protease: the R355 gene product. Its expression in E. coli, its crystallization and the preliminary phasing of a MAD data set using the selenium signal present in a crystal of recombinant selenomethionine-substituted protein are reported. Online 24 December 2010 |
Acta Cryst. (2011). F67, 173-177 [ doi:10.1107/S1744309110045318 ] Notes for authors 2011Online 24 December 2010 |
Copyright © International Union of Crystallography
IUCr Webmaster