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Cover illustration: View of several protein crystals in their plates or isolated. The proteins are produced from unknown ORFs of E. coli, within a structural genomics programme. The crystals were obtained with a nanodrop dispensing robot. The initial volume of the drops was 100 + 100 nl. Most crystals appeared between 4 and 48 h (p. 2109). |
Acta Cryst. (2002). D58, 1971 [ doi:10.1107/S0907444902021273 ] EditorialJ. P. GluskerOnline 26 November 2002 |
Acta Cryst. (2002). D58, 1972-1982 [ doi:10.1107/S0907444902016566 ] The structures of Micrococcus lysodeikticus catalase, its ferryl intermediate (compound II) and NADPH complexG. N. Murshudov, A. I. Grebenko, J. A. Brannigan, A. A. Antson, V. V. Barynin, G. G. Dodson, Z. Dauter, K. S. Wilson and W. R. Melik-AdamyanSynopsis: The crystal structure of the bacterial catalase from M. lysodeikticus has been refined at 0.88 Å using the gene-derived sequence, revealing the active site with unprecedented accuracy. In addition, the structures of the ferryl intermediate of the catalase (compound II) at 1.96 Å resolution and the catalase complex with NADPH at 1.83 Å resolution have been determined. PDB references: 1gwe, 1hbz, 1gwf and 1gwh Online 26 November 2002 |
Acta Cryst. (2002). D58, 1983-1991 [ doi:10.1107/S090744490201394X ] The impact of Glu
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Acta Cryst. (2002). D58, 1992-2000 [ doi:10.1107/S0907444902015433 ] Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound stateS. Parthasarathy, H. Balaram, P. Balaram and M. R. N. MurthySynopsis: Structures of triosephosphate isomerase (TIM) from the malarial parasite P. falciparum (Pf) complexed to the substrate analogues 3-phosphoglycerate and glycerol-3-phosphate have been determined at 2.4 Å resolution. The catalytic loop of TIM adopts a novel `loop-open' conformation in these complexes. These structures provide insight into the design of inhibitors specific for the malarial enzyme. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2001-2008 [ doi:10.1107/S0907444902014695 ] Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8 Å in complex with the inhibitors rs367 and rs370O. A. Asojo, E. Afonina, S. V. Gulnik, B. Yu, J. W. Erickson, R. Randad, D. Medjahed and A. M. SilvaSynopsis: Two 1.8 Å resolution crystal structures of the Ser205 mutant plasmepsin II from P. falciparum in complex with two Phe-Leu core inhibitors that incorporate tetrahedral transition-state mimetic hydroxypropylamine are described. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2009-2017 [ doi:10.1107/S0907444902014683 ] Refinement of the arginine kinase transition-state analogue complex at 1.2 Å resolution: mechanistic insightsM. S. Yousef, F. Fabiola, J. L. Gattis, T. Somasundaram and M. S. ChapmanSynopsis: The transition-state complex of this 42 kDa homologue of creatine kinase has been refined at 1.2 Å resolution. It indicates that precise positioning of substrates and restriction of the active-site motion are important components in catalysis. PDB reference: 1m15 Online 26 November 2002 |
Acta Cryst. (2002). D58, 2018-2023 [ doi:10.1107/S0907444902015548 ] Structure of a circularly permuted phosphoglycerate kinaseP. Tougard, T. Bizebard, M. Ritco-Vonsovici, P. Minard and M. DesmadrilSynopsis: The crystallographic structure of a circularly permuted form of yeast PGK has been determined to a resolution of 2.3 Å. The overall fold of the protein is very similar to that of the wild-type protein, directly demonstrating that the continuity of a folding unit is not relevant to the folding process of the whole protein. PDB reference: 1fw8 Online 26 November 2002 |
Acta Cryst. (2002). D58, 2024-2030 [ doi:10.1107/S0907444902015524 ] An investigation of magnetic field effects on the dissolution of lysozyme crystal and related phenomenaD. C. Yin, Y. Inatomi, N. I. Wakayama, W. D. Huang and K. KuribayashiSynopsis: The diffusivity of lysozyme molecules was deduced to decrease under a magnetic field, based on the discovery of magnetic damping of the dissolution process using a Mach-Zehnder interferometer. In the same experiment, a redistribution of the concentration before crystal growth was also found. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2031-2037 [ doi:10.1107/S0907444902015809 ] Structure of human carbonmonoxyhemoglobin at 2.16 Å: a snapshot of the allosteric transitionM. K. Safo, J. C. Burnett, F. N. Musayev, S. Nokuri and D. J. AbrahamSynopsis: A new structure of carbonmonoxyhemoglobin solved at 2.16 Å is reported. The new structure, obtained using a lower pH, shows significant strain at the PDB reference: 1ljw Online 26 November 2002 |
Acta Cryst. (2002). D58, 2038-2042 [ doi:10.1107/S0907444902016426 ] Structure of mutant human carbonmonoxyhemoglobin C (
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Acta Cryst. (2002). D58, 2043-2054 [ doi:10.1107/S0907444902016724 ] Automatic modeling of protein backbones in electron-density maps via prediction of C
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Acta Cryst. (2002). D58, 2055-2059 [ doi:10.1107/S0907444902017420 ] Structure determination of a cocaine hydrolytic antibody from a pseudomerohedrally twinned crystalN. A. Larsen, A. Heine, P. de Prada, E.-R. Redwan, T. O. Yeates, D. W. Landry and I. A. WilsonSynopsis: The structure of a cocaine hydrolytic antibody has been determined from a pseudomerohedrally twinned crystal. The lattice is primitive monoclinic with higher apparent primitive orthorhombic symmetry. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2060-2065 [ doi:10.1107/S0907444902017183 ] Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatinC. Charron, A. Kadri, M.-C. Robert, R. Giegé and B. LorberSynopsis: Glycerol displaces water molecules bound to thaumatin. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2066-2075 [ doi:10.1107/S0907444902016992 ] Multiple rotation functionA. Urzhumtsev and L. UrzhumtsevaSynopsis: A simultaneous analysis of several rotation functions allows the model orientation to be found in situations when the standard search fails. An automated procedure has been developed to apply such an analysis routinely. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2076-2081 [ doi:10.1107/S0907444902016736 ] The influence of detergents on the solubility of membrane proteinsM. A. Rosenow, C. L. Magee, J. C. Williams and J. P. AllenSynopsis: The dependence of protein solubility on ionic strength was measured for the bacterial reaction center in different detergents and amphiphiles. The detergent and amphiphile combinations that yielded the highest solubility of the protein are correlated with those that yield protein crystals. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2082-2086 [ doi:10.1107/S0907444902016360 ] Statistical density modification with non-crystallographic symmetryT. C. TerwilligerSynopsis: Statistical density modification can make use of NCS in a crystal and can include estimates of the deviations from perfect NCS. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2087-2095 [ doi:10.1107/S0907444902017511 ] Convergent-beam method in macromolecular crystallographyJ. X. Ho, J. R. Ruble, T. R. McInnis, D. C. Carter, H. Huang and W. M. GibsonSynopsis: The convergent-beam method of data collection for macromolecular crystals is described. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2096-2101 [ doi:10.1107/S0907444902018838 ] S-SAD, Se-SAD and S/Se-SIRAS using Cu K
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Acta Cryst. (2002). D58, 2102-2108 [ doi:10.1107/S0907444902016359 ] Parallel cloning, expression, purification and crystallization of human proteins for structural genomicsH. Ding, H. Ren, Q. Chen, G. Fang, L. Li, R. Li, Z. Wang, X. Jia, Y. Liang, M. Hu, Y. Li, J. Luo, X. Gu, X.-D. Su, M. Luo and S. LuSynopsis: Insights are gained into high-throughput target selection, cloning, expression and crystallization of human genomic proteins. For example, there was a marked difference seen bewteen the ease of expression of proteins of molecular weight (MW) < 25 kDa (93% success), compared with proteins > 25 kDa MW, which were less easy to express (61% success). Online 26 November 2002 |
Acta Cryst. (2002). D58, 2109-2115 [ doi:10.1107/S0907444902013938 ] A medium-throughput crystallization approachG. Sulzenbacher, A. Gruez, V. Roig-Zamboni, S. Spinelli, C. Valencia, F. Pagot, R. Vincentelli, C. Bignon, A. Salomoni, S. Grisel, D. Maurin, C. Huyghe, K. Johansson, A. Grassick, A. Roussel, Y. Bourne, S. Perrier, L. Miallau, P. Cantau, E. Blanc, M. Genevois, A. Grossi, A. Zenatti, V. Campanacci and C. CambillauSynopsis: In the context of a medium-scale structural genomics program, a crystallization approach was based on a two-step procedure: a large screening step employing robotics, followed by manual or automated optimization of the crystallization conditions. A nanodrop dispensing robot (50-200 nl) proved to be useful for obtaining diffracting crystals while using small amounts of protein. In 10 months, 25 proteins were subjectred to crystallization, 13 yielded crystals among which ten led to usuable data sets and five to structures. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2116-2121 [ doi:10.1107/S0907444902017055 ] Autotracing of Escherichia coli acetate CoA-transferase
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Acta Cryst. (2002). D58, 2122-2124 [ doi:10.1107/S0907444902011204 ] Purification, crystallization and preliminary X-ray analysis of the disintegrin contortrostatin from Agkistrodon contortrix contortrix snake venomN. Moiseeva, S. D. Swenson, F. S. Markland Jr and R. BauSynopsis: Contortrostatin, a small homodimeric protein (64 residues per chain) from southern copperhead snake venom, has been crystallized successfully. Crystals of the title compound, which is a member of the disintegrin family of proteins, diffract up to a maximum resolution of 1.7 Å. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2125-2126 [ doi:10.1107/S0907444902015469 ] Crystallization of an
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Acta Cryst. (2002). D58, 2127-2130 [ doi:10.1107/S0907444902015020 ] Crystallographic studies of a novel DNA-binding domain from the yeast transcriptional activator Ndt80S. P. Montano, M. Pierce, M. L. Coté, A. K. Vershon and M. M. GeorgiadisSynopsis: The Ndt80 protein is a transcriptional activator that plays a key role in the progression of the meiotic divisions in the yeast Saccharomyces cerevisiae. Crystals of the DNA-binding domain of Ndt80 in two distinct lattices have been obtained, for which diffraction data extend to 2.3 Å resolution. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2131-2134 [ doi:10.1107/S0907444902015482 ] The production, purification and crystallization of a soluble heterodimeric form of a highly selected T-cell receptor in its unliganded and liganded stateC. S. Clements, L. Kjer-Nielsen, W. A. MacDonald, A. G. Brooks, A. W. Purcell, J. McCluskey and J. RossjohnSynopsis: This report details the production, purification, crystallization and preliminary diffraction analysis of a T-cell receptor. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2135-2137 [ doi:10.1107/S0907444902015494 ] Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding domain of flocculin, a cell-adhesion molecule from Saccharomyces carlsbergensisM. Groes, K. Teilum, K. Olesen, F. M. Poulsen and A. HenriksenSynopsis: The recombinant carbohydrate-binding domain of the cell-surface lectin flocculin from brewer's yeast has been identified, purified and crystallized. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2138-2140 [ doi:10.1107/S0907444902015512 ] Crystallization and preliminary X-ray analysis of the ytxM gene product from Bacillus subtilisM. M. Mehanni, A. P. Turnbull, S. E. Sedelnikova, P. J. Baker, S. Foster and D. W. RiceSynopsis: The B. subtilis ytxM gene product has been crystallized and a MAD data set has been collected to 2.0 Å resolution. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2141-2144 [ doi:10.1107/S0907444902015536 ] Crystallization and preliminary X-ray analysis of the tumor metastasis factor p37R. Reutzel, S. K. Boehlein, L. Govindasamy, R. B. Brenes, M. Agbandje-McKenna, S. M. Schuster and R. McKennaSynopsis: P37, an outer-membrane bacterial protein from Mycoplasma hyorhinis whose presence on the surface of many tumor cells correlates highly with increased neoplastic invasivity and metastasis, has been overexpressed in Escherichia coli, purified by affinity chromatography and crystallized. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2145-2146 [ doi:10.1107/S0907444902015573 ] Crystallization and preliminary X-ray crystallographic analysis of acetohydroxy acid isomeroreductase from Pseudomonas aeruginosaS. J. Eom, H. J. Ahn, H.-J. Yoon, B. I. Lee, S. H. Bae, S. H. Baek and S. W. SuhSynopsis: Acetohydroxy acid isomeroreductase from P. aeruginosa was crystallized. X-ray data have been collected to 2.0 Å resolution using synchrotron radiation (P213, a = b = c = 184.38 Å). Online 26 November 2002 |
Acta Cryst. (2002). D58, 2147-2149 [ doi:10.1107/S090744490201572X ] Crystallization and preliminary X-ray analysis of the trehalose/maltose ABC transporter MalFGK2 from Thermococcus litoralisA. Schiefner, K. Diederichs, K. Hashimoto, W. Boos and W. WelteSynopsis: The crystallization and preliminary characterization of the MalFGK2 transport complex from T. litoralis is presented. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2150-2152 [ doi:10.1107/S0907444902015743 ] Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of Pseudomonas aeruginosa L-arginine deiminaseY. Oudjama, C. Tricot, V. Stalon and J. WoutersSynopsis: Overexpression, purification and crystallization of P. aeruginosa L-arginine deiminase allowed collection of a complete MAD data set to 3.2 Å resolution. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2153-2156 [ doi:10.1107/S090744490201569X ] Co-crystallization of Staphylococcus aureus peptide deformylase (PDF) with potent inhibitorsM. S. Harris, J. H. Bock, G. Choi, J. S. Cialdella, K. A. Curry, M. R. Deibel Jr, E. J. Jacobsen, V. P. Marshall, R. W. Murray Jr, A. F. Vosters, C. L. Wolfe, A. W. Yem and E. T. BaldwinSynopsis: Diffraction-quality Se-met crystals of S. aureus PDF were prepared that belong to space group C2221 with unit-ell parameters of a = 94.1 b = 121.9 c = 47.6 Å. Crystals were also prepared with three PDF inhibitors: thiorphan, actinonin and PNU-172550. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2157-2158 [ doi:10.1107/S0907444902015810 ] Crystallization and preliminary X-ray diffraction studies of NusG, a protein shared by the transcription and translation machinesM. Andrykovitch, W. Guo, K. M. Routzahn, Y. Gu, D. E. Anderson, L. S. Reshetnikova, J. R. Knowlton, D. S. Waugh and X. JiSynopsis: N-utilization factor G (NusG) from A. aeolicus has been overexpressed, purified and crystallized. The crystals diffract to 2.45 Å resolution. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2159-2161 [ doi:10.1107/S0907444902015858 ] Cloning, expression, purification and preliminary X-ray crystallographic studies of 2-methylisocitrate lyase from Salmonella typhimuriumD. K. Simanshu, P. S. Satheshkumar, S. Parthasarathy, H. S. Savithri and M. R. N. MurthySynopsis: 2-Methylisocitrate lyase from S. typhimurium IFO 12529 has been cloned, overexpressed and crystallized. The crystal belongs to space group P212121, with unit-cell parameters a = 63.600, b = 100.670, c = 204.745 Å. A complete data set to 2.5 Å resolution has been collected. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2162-2164 [ doi:10.1107/S0907444902016050 ] Crystallization and preliminary X-ray structure analysis of isocitrate dehydrogenase from two hyperthermophiles, Aeropyrum pernix and Thermotoga maritimaM. Karlström, I. H. Steen, G. Tibbelin, T. Lien, N.-K. Birkeland and R. LadensteinSynopsis: Extremely thermostable isocitrate dehydrogenases from A. pernix and T. maritima were crystallized and X-ray diffraction data were collected to 2.6 and 2.8 Å, respectively. The crystallization and preliminary crystallographic analysis are described for both enzymes. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2165-2167 [ doi:10.1107/S0907444902016062 ] Purification, characterization and preliminary crystallographic studies of a PR-10 protein from Pachyrrhizus erosus seedsF. Wu, Y. Li, S. Chang, Z. Zhou, F. Wang, X. Song, Y. Lin and W. GongSynopsis: A new PR-10 family protein SPE16 with ribonuclease activity was purified from the seeds of P. erosus as a constitutive protein and has been crystallized. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2168-2169 [ doi:10.1107/S0907444902016396 ] Crystallization and preliminary X-ray diffraction analysis of FKBP52 N-terminal domainP. Li, C. Shu, B. Wu, Y. Ding, B. Shen and Z. RaoSynopsis: The N-terminal (amino acids 1-140) domain of human FKBP52 has been crystallized. The crystals belong to space group P21 with unit-cell parameters a = 27.8, b = 58.4, c = 70.9 Å, Online 26 November 2002 |
Acta Cryst. (2002). D58, 2170-2172 [ doi:10.1107/S090744490201644X ] Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of human dok-5 proteinN. Shi, W. Zhou, K. Tang, Y. Gao, J. Jin, F. Gao, X. Peng, M. Bartlam, B. Qiang, J. Yuan and Z. RaoSynopsis: The PTB domain of human dok-5 protein has been crystallized as well as a selenomethionmine-substituted protein for MAD phasing determination. The crystals belong to space group P3221 (a = b = 75.9, c = 108.0 Å) and diffract up to 2.3 Å resolution using synchrotron radiation. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2173-2174 [ doi:10.1107/S0907444902016803 ] Crystallization and preliminary X-ray diffraction analysis of naphthalene dioxygenase from Rhodococcus sp. strain NCIMB 12038Z. A. Malik, C. C. R. Allen, L. Gakhar, D. A. Lipscomb, M. J. Larkin and S. RamaswamySynopsis: Naphthalene dioxygenase from Rhodococcus has been crystallized in space group P212121. The crystals diffract to 2.3 Å resolution. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2175-2176 [ doi:10.1107/S0907444902016815 ] Crystallization and preliminary X-ray diffraction analysis of a thermostable D-hydantoinase from the mesophilic Bacillus sp. AR9V. Agrawal, R. Sharma, R. M. Vohra and K. V. R. KishanSynopsis: A thermostable D-hydantoinase from mesophilic Bacillus sp. AR9 was crystallized and diffracted to 2.3 Å resolution having unit-cell parameters a = b = 129.55, c = 102.8 Å, Online 26 November 2002 |
Acta Cryst. (2002). D58, 2177-2179 [ doi:10.1107/S0907444902016827 ] Crystallization of Pichia pastoris lysyl oxidaseM. Lee, K. Willingham, D. Langley, M. J. Maher, A. E. Cohen, P. J. Ellis, J. A. Kuchar, D. M. Dooley, H. C. Freeman and J. M. GussSynopsis: The lysyl oxidase isolated from the yeast P. pastoris has been crystallized and synchrotron data have been recorded to a resolution of 1.65 Å. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2180-2181 [ doi:10.1107/S0907444902017067 ] Preliminary crystallographic studies of the creatinine amidohydrolase from Pseudomonas putidaK. Ito, N. Kanada, T. Inoue, K. Furukawa, K. Yamashita, N. Tanaka, K. T. Nakamura, Y. Nishiya, A. Sogabe and T. YoshimotoSynopsis: Creatinine amidohydrolase (creatininase; EC 3.5.2.10) from P. putida has been overexpressed in E. coli and crystallized by the hanging-drop method. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2182-2183 [ doi:10.1107/S0907444902017432 ] Crystallization and preliminary X-ray crystallographic studies on the class II cholesterol oxidase from Burkholderia cepacia containing bound flavinR. Aunpad, S. P. Muench, P. J. Baker, S. Sedelnikova, W. Panbangred, N. Doukyu, R. Aono and D. W. RiceSynopsis: Crystals of B. cepacia cholesterol oxidase, a 3 Online 26 November 2002 |
Acta Cryst. (2002). D58, 2184-2186 [ doi:10.1107/S0907444902017869 ] Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomalleiX. Carpena, J. Switala, S. Loprasert, S. Mongkolsuk, I. Fita and P. C. LoewenSynopsis: Crystals of the catalase-peroxidase from B. pseudomallei diffract to beyond 1.8 Å. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2187-2190 [ doi:10.1107/S0907444902017535 ] Expression, purification, crystallization and preliminary X-ray diffraction studies of human cathepsin F complexed with an irreversible vinyl sulfone inhibitorJ. D. Ho, Y. Meltser, J. J. Buggy, J. T. Palmer, K. C. Elrod, H. Chan, K. D. Mortara and J. R. SomozaSynopsis: A human papain-family cysteine protease has been expressed in P. pastoris, purified by conventional chromatography and crystallized. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2191-2193 [ doi:10.1107/S0907444902017894 ] Expression, purification, crystallization and preliminary characterization of an HHED aldolase homologue from Escherichia coli K12A. Wright, A. Blewett, V. Fulop, R. Cooper, S. Burrows, C. Jones and D. RoperSynopsis: An ORF from the E. coli K12 genome with 56% sequence identity to 2,4-dihydroxy-hept-2-ene-1,7-dioic acid (HHED) aldolase has been cloned, expressed and purified. Crystals obtained from the purified recombinant enzyme, belonging to space group C2221, diffracted to a resolution of 1.78 Å. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2194-2197 [ doi:10.1107/S0907444902015445 ] Co-crystallization of the human nuclear cap-binding complex with a m7GpppG cap analogue using protein engineeringC. Mazza, A. Segref, I. W. Mattaj and S. CusackSynopsis: A long solvent-exposed coiled coil in the large subunit (CBP80) of the heterodimeric nuclear cap-binding complex (CBC) has been truncated to permit crystallization of CBC with the cap analogue m7GpppG in two crystal forms diffracting to 2.15 and 2.3 Å resolution. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2198-2200 [ doi:10.1107/S0907444902015457 ] The 2.2 Å resolution structure of thermolysin (TLN) crystallized in the presence of potassium thiocyanateJ.-F. Gaucher, M. Selkti, T. Prangé and A. TomasSynopsis: The structure of the thermolysin (TLN) crystallized in the presence of SCN- suggests explanations for the solubility increase of TLN and for the inhibitory effect of high SCN- concentrations on the TLN activity. PDB reference: 1gxw Online 26 November 2002 |
Acta Cryst. (2002). D58, 2201-2204 [ doi:10.1107/S0907444902017006 ] Structure of the Humicola insolens cellobiohydrolase Cel6A D416A mutant in complex with a non-hydrolysable substrate analogue, methyl cellobiosyl-4-thio-
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Acta Cryst. (2002). D58, 2205-2208 [ doi:10.1107/S0907444902015500 ] When pseudosymmetry and merohedral twinning come across: the case of the d(ApTpApTpApT) oligonucleotide in a hexagonal latticeN. G. A. Abrescia and J. A. SubiranaSynopsis: Crystallization analyasis of twinned diffraction data of d(ApTpApTpApT) in a hexagonal packing. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2209-2212 [ doi:10.1107/S0907444902016402 ] Structure of Escherichia coli pyruvate formate-lyase with pyruvateL. Lehtiö, V.-M. Leppänen, J. W. Kozarich and A. GoldmanSynopsis: The structure of inactive pyruvate formate-lyase in complex with a natural substrate, pyruvate, has been solved at 2.7 Å resolution. PDB reference: 1mzo Online 26 November 2002 |
Acta Cryst. (2002). D58, 2213-2215 [ doi:10.1107/S0907444902016384 ] Rapid automatic NCS identification using heavy-atom substructuresT. C. TerwilligerSynopsis: A rapid algorithm for identifying NCS in heavy-atom sites is described. Online 26 November 2002 |
Acta Cryst. (2002). D58, 2216 [ doi:10.1107/S0907444902019790 ] FOX two-dimensional X-ray focusing opticOnline 26 November 2002 |
Acta Cryst. (2002). D58, 2216 [ doi:10.1107/S0907444902021261 ] New developments in protein-crystallization platforms and barcoding for cryogenic storageOnline 26 November 2002 |
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