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Cover illustration: Human acetylcholinesterase complexed with fasciculin-II. hAChE is shown as a solvent-accessible surface in gold and FAS-II is shown as a ribbon in green. The red area corresponds to points on the surface 4 Å from FAS-II and the inner surface of the active-site gorge is coloured grey (p. 1385). |
Acta Cryst. (2000). D56, 1359-1366 [ doi:10.1107/S0907444900009537 ] Cloning, sequence and crystallographic structure of recombinant iron superoxide dismutase from Pseudomonas ovalisC. J. Bond, J. Huang, R. Hajduk, K. E. Flick, P. J. Heath and B. L. StoddardSynopsis: The gene encoding iron superoxide dismutase from P. ovalis has been cloned and sequenced; the recombinant enzyme has been crystallized and its structure determined. PDB reference: 1dt0 Online November 2000 |
Acta Cryst. (2000). D56, 1367-1375 [ doi:10.1107/S0907444900009896 ] Structure of XynB, a highly thermostable
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Acta Cryst. (2000). D56, 1376-1384 [ doi:10.1107/S0907444900010647 ] Structure of the C123S mutant of dienelactone hydrolase (DLH) bound with the PMS moiety of the protease inhibitor phenylmethylsulfonyl fluoride (PMSF)A. Robinson, K. J. Edwards, P. D. Carr, J. D. Barton, G. D. Ewart and D. L. OllisSynopsis: The structure of the DLH (C123S) with PMS bound indicates that the reason the enzyme is able to catalyse a wide range of dissimilar substrates is a consequence of its capacity to undergo a coordinated restructuring of the active site and associated regions of the molecule without compromising the stability of its tertiary fold. PDB reference: 1ggv Online November 2000 |
Acta Cryst. (2000). D56, 1385-1394 [ doi:10.1107/S0907444900010659 ] Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-IIG. Kryger, M. Harel, K. Giles, L. Toker, B. Velan, A. Lazar, C. Kronman, D. Barak, N. Ariel, A. Shafferman, I. Silman and J. L. SussmanSynopsis: The structures of recombinant wild-type human acetylcholinesterase and of its E202Q mutant, as complexes with fasciculin-II, a `three-finger' snake neurotoxin, have been determined to 2.8 and 2.7 Å resolution, respectively. The overall structures of these complexes are similar to those of the Torpedo and mouse enzymes with fasciculin-II. Comparison of the wild-type and the mutant structures shows that removal of the charged group from the protein core, and its substitution by a neutral isosteric moiety, does not disrupt the functional architecture of the active center. Online November 2000 |
Acta Cryst. (2000). D56, 1395-1400 [ doi:10.1107/S0907444900010763 ] Structure of human
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Acta Cryst. (2000). D56, 1401-1407 [ doi:10.1107/S0907444900011501 ] The atomic resolution structure of bucandin, a novel toxin isolated from the Malayan krait, determined by direct methodsP. Kuhn, A. M. Deacon, S. Comoso, G. Rajaseger, R. M. Kini, I. Usón and P. R. KolatkarSynopsis: The structure of bucandin, a novel three-finger toxin, has been determined by direct methods. The full-matrix least-squares refinement to atomic resolution, with anisotropic temperature factors, converged to an R factor of 12.4%. PDB reference: 1f94 Online November 2000 |
Acta Cryst. (2000). D56, 1408-1412 [ doi:10.1107/S0907444900010052 ] Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin moleculeR. Morales, G. Kachalova, F. Vellieux, M.-H. Charon and M. FreySynopsis: The first structure of a complex between ferredoxin-NADP+ reductase and ferredoxin has been solved at 2.4 Å resolution by molecular replacement, anomalous dispersion and Rmin search methods. The crystal was treated as a merohedral twin. PDB reference: 1ewy Online November 2000 |
Acta Cryst. (2000). D56, 1413-1420 [ doi:10.1107/S0907444900010039 ] Single-wavelength anomalous diffraction phasing revisitedL. M. Rice, T. N. Earnest and A. T. BrungerSynopsis: Analyzing the anomalous diffraction from seven different selenomethionine-labelled crystals, we show that the combination of single-wavelength anomalous-diffraction phasing and solvent flattening is sufficient to unambiguously determine most structures. Online November 2000 |
Acta Cryst. (2000). D56, 1421-1429 [ doi:10.1107/S0907444900011227 ] Evaluation of phase accuracy via topological and geometrical analysis of electron-density mapsC. Colovos, E. A. Toth and T. O. YeatesSynopsis: A systematic analysis of local and global protein electron-density map properties is used to derive an empirical function to measure the average error in diffraction phase sets. Online November 2000 |
Acta Cryst. (2000). D56, 1430-1431 [ doi:10.1107/S0907444900011203 ] Evaporative microdialysis: an effective improvement in an established method of protein crystallizationC. Bunick, A. C. T. North and G. StubbsSynopsis: Slow evaporation of the reservoir in microdialysis can lead to a significant increase in the crystal size of proteins for which the crystallization region of supersaturation is particularly limited. Online November 2000 |
Acta Cryst. (2000). D56, 1432-1433 [ doi:10.1107/S0907444900010064 ] Crystallization and preliminary crystallographic study of an extremophile cytochrome c4 from Thiobacillus ferrooxidansC. Abergel, M. Bruschi, S. Chenivesse, S. Guasco, G. Leroy and M.-T. Guidici-OrticoniSynopsis: The acidic cytochrome c4 from T. ferrooxidans has been cloned, expressed, purified and crystallized. The MAD method using the four Fe per asymmetric unit is used to solve the protein structure. Online November 2000 |
Acta Cryst. (2000). D56, 1434-1436 [ doi:10.1107/S0907444900009719 ] Crystallization and preliminary X-ray diffraction analysis of a eumenine mastoparan toxin: a new class of mast-cell degranulating peptide in the wasp venomF. Canduri, P. Delatorre, V. Fadel, C. C. B. Lorenzi, J. H. Pereira, J. R. Olivieri, J. Ruggiero Neto, K. Konno, M. S. Palma, T. Yamane and W. F. de AzevedoSynopsis: The crystallization and preliminary X-ray analysis of a mastoparan peptide isolated from the venom of the solitary wasp A. flavomarginatum micado is reported. Online November 2000 |
Acta Cryst. (2000). D56, 1437-1439 [ doi:10.1107/S0907444900009859 ] Preliminary crystallographic studies of an extremely thermostable KDG aldolase from Sulfolobus solfataricusE. J. Hendry, C. L. Buchanan, R. J. M. Russell, D. W. Hough, C. D. Reeve, M. J. Danson and G. L. TaylorSynopsis: The growth of three crystal forms of 2-keto-3-deoxygluconate aldolase from the hyperthermophilic archaeon S. solfataricus is reported. Online November 2000 |
Acta Cryst. (2000). D56, 1440-1442 [ doi:10.1107/S0907444900009884 ] Crystallization and preliminary X-ray diffraction analysis of a recombinant cysteine-free mutant of crmAM. Simonovic, P. G. W. Gettins and K. VolzSynopsis: The first crystallization of a serpin that is either viral or a cysteine proteinase inhibitor is described. Online November 2000 |
Acta Cryst. (2000). D56, 1443-1445 [ doi:10.1107/S090744490000994X ] Crystallization and preliminary X-ray analysis of glucose dehydrogenase from Bacillus megaterium IWG3K. Yamamoto, M. Kusunoki, I. Urabe, S. Tabata and S. OsakiSynopsis: Glucose dehydrogenase from B. megaterium IWG3 has been crystallized and 1.7 Å resolution data have been collected using a synchrotron-radiation source. Online November 2000 |
Acta Cryst. (2000). D56, 1446-1448 [ doi:10.1107/S0907444900009951 ] Crystallization and preliminary X-ray crystallographic studies of response regulator for cyanobacterial phytochrome, Rcp1Y. J. Im, C.-M. Park, J.-I. Kim, S.-S. Yang, J.-G. Kang, S.-H. Rho, J. I. Kim, W. K. Song, P.-S. Song and S. H. EomSynopsis: The key response regulator of light regulation, Rcp1, from Synechocystis sp. has been crystallized in a form suitable for X-ray diffraction studies. The crystals belong to space group P63 and diffracted to 2.5 Å. Online November 2000 |
Acta Cryst. (2000). D56, 1449-1451 [ doi:10.1107/S0907444900010027 ] Expression, crystallization and preliminary X-ray diffraction studies of recombinant Bacillus anthracis lethal factorL. Bernardi, G. Vitale, C. Montecucco and A. MusacchioSynopsis: The lethal factor (LF) produced by toxigenic strains of B. anthracis is a Zn-endopeptidase responsible of the lethal effects of anthrax. LF has been expressed in E. coli as recombinant GST fusion, purified and crystallized; preliminary crystallographic studies are described. Online November 2000 |
Acta Cryst. (2000). D56, 1452-1455 [ doi:10.1107/S0907444900010143 ] Crystallization and preliminary X-ray diffraction analysis of a functional form of pneumolysin, a virulence factor from Streptococcus pneumoniaeS. J. Kelly and M. J. JedrzejasSynopsis: Crystals of a functional form of pneumolysin, a virulence factor of S. pneumoniae, have been obtained in complex with its activator, a cholesterol molecule, by the vapor-diffusion method. The crystallization process as well as the preliminary X-ray analysis are discussed. Online November 2000 |
Acta Cryst. (2000). D56, 1456-1458 [ doi:10.1107/S0907444900010295 ] Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the multidrug transporter activation protein (MtaN) from Bacillus subtilisM. H. Godsey, N. N. Baranova, A. A. Neyfakh and R. G. BrennanSynopsis: The DNA-binding domain of the MerR family member MtaN has been crystallized in space group I212121. Intensity data have been collected from these crystals at 100 K at a synchrotron-radiation source to 2.75 Å resolution. Online November 2000 |
Acta Cryst. (2000). D56, 1459-1461 [ doi:10.1107/S0907444900010301 ] Crystallization and preliminary X-ray analysis of full-length annexin I comprising the core and N-terminal domainA. Rosengarth and H. LueckeSynopsis: Annexin I, a member of the annexin family of Ca2+- and phospholipid-binding proteins, has been crystallized with the complete N-terminus. Online November 2000 |
Acta Cryst. (2000). D56, 1462-1463 [ doi:10.1107/S0907444900010374 ] Crystallization and preliminary X-ray analysis of a bacterial lysozyme produced by Streptomyces globisporusT. Shiba, S. Harada, H. Sugawara, H. Naitow, Y. Kai and Y. SatowSynopsis: A bacterial lysozyme produced by S. globisporus was crystallized in space group P41212, with unit-cell parameters a = 63.11, c = 121.1 Å. A clear molecular-replacement solution was obtained and the structure refinement is in progress. Online November 2000 |
Acta Cryst. (2000). D56, 1464-1465 [ doi:10.1107/S0907444900010386 ] Expression, purification and crystallization of human tau-protein kinase I/glycogen synthase kinase-3
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Acta Cryst. (2000). D56, 1466-1467 [ doi:10.1107/S0907444900010660 ] Crystallization and preliminary crystallographic studies of trichomaglin, a novel ribosome-inactivating proteinJ. Wu, J.-H. Gan and Z.-X. XiaSynopsis: Trichomaglin has been crystallized in two crystal forms. Online November 2000 |
Acta Cryst. (2000). D56, 1468-1469 [ doi:10.1107/S0907444900010738 ] Crystallization and preliminary X-ray analysis of CTLA-4 (CD152) membrane-external domainC. Y. Chang, W. H. Fenderson, T. B. Lavoie, R. J. Peach, H. M. Einspahr and S. SheriffSynopsis: The membrane-external domain of the immune modulator CTLA-4 (CD152) has been crystallized; the crystals diffract to 2.7 Å resolution at synchrotron sources. Online November 2000 |
Acta Cryst. (2000). D56, 1470-1472 [ doi:10.1107/S090744490001074X ] Crystallization and preliminary X-ray crystallographic studies of the thermoactive pullulanase type I, hydrolyzing
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Acta Cryst. (2000). D56, 1473-1475 [ doi:10.1107/S0907444900010702 ] Crystallization and preliminary X-ray crystallographic studies on the bacteriophage
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Acta Cryst. (2000). D56, 1476-1478 [ doi:10.1107/S0907444900010714 ] Crystallization and preliminary X-ray analysis of the auxin receptor ABP1E.-J. Woo, J. Bauly, J.-G. Chen, J. Marshall, H. Macdonald, C. Lazarus, P. Goodenough, M. Venis, R. Napier and R. PickersgillSynopsis: Monoclinic crystals of the maize auxin receptor ABP1 diffract to 1.9 Å resolution. Online November 2000 |
Acta Cryst. (2000). D56, 1479-1481 [ doi:10.1107/S0907444900010957 ] Purification, crystallization and preliminary X-ray crystallographic analysis of human CCG1-interacting factor BB. Padmanabhan, T. Kuzuhara, H. Mizuno and M. HorikoshiSynopsis: Preliminary crystal data have been obtained for the first time for human CCG1-interacting factor B. The results of preliminary X-ray diffraction are discussed. Online November 2000 |
Acta Cryst. (2000). D56, 1482-1484 [ doi:10.1107/S0907444900011136 ] Crystallization and preliminary X-ray diffraction studies of a new crystal form of human secretory type IIA phospholipase A2W. B. Church, P.-W. Lei, D. J. Ogg and K. F. ScottSynopsis: Preliminary crystal data have been obtained for a new crystal form of human secretory phospholipase A2 IIA crystallized with pentapeptide inhibitors. The enzyme crystallizes in space group C2, with unit-cell parameters a = 140.8, b = 38.9, c = 109.1 Å, Online November 2000 |
Acta Cryst. (2000). D56, 1485-1487 [ doi:10.1107/S0907444900011240 ] Nucleoside diphosphate kinase from the hyperthermophilic archaeon Methanococcus jannaschii: overexpression, crystallization and preliminary X-ray crystallographic analysisK. Min, H. K. Song, C. Chang, J. Y. Lee, S. H. Eom, K. K. Kim, Y. G. Yu and S. W. SuhSynopsis: Nucleoside diphosphate kinase from M. jannaschii has been crystallized using polyethylene glycol 4000 as precipitant. Native data have been collected to 2.30 Å resolution using synchrotron X-rays. Online November 2000 |
Acta Cryst. (2000). D56, 1488-1491 [ doi:10.1107/S0907444900011306 ] Purification, crystallization and preliminary X-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coliB. Lohkamp, J. R. Coggins and A. J. LapthornSynopsis: Crystals of ATP-phosphoribosyltransferase from E. coli were obtained by the vapour-diffusion method and diffract to 2.7 Å. The quaternary structure is determined based on the preliminary crystallographic studies. Online November 2000 |
Acta Cryst. (2000). D56, 1492-1494 [ doi:10.1107/S0907444900011380 ] Preliminary X-ray diffraction studies of rabbit muscle triose phosphate isomerase (TIM)R. Aparicio, S. T. Ferreira, N. R. Leite and I. PolikarpovSynopsis: Here the crystallization, data collection and molecular-replacement solutions obtained for two crystalline forms of triose phosphate isomerase, one determined at 85 K and the other at 298 K are reported. Online November 2000 |
Acta Cryst. (2000). D56, 1495-1497 [ doi:10.1107/S0907444900011446 ] Cloning, expression, purification and crystallization of dihydroxybutanone phosphate synthase from Magnaporthe griseaD.-I. Liao, P. V. Viitanen and D. B. JordanSynopsis: Dihydroxybutanone phosphate synthase from M. grisea was cloned, expressed and crystallized. Crystals diffract to 1.0 Å resolution. Online November 2000 |
Acta Cryst. (2000). D56, 1498-1500 [ doi:10.1107/S0907444900011744 ] Crystallization and preliminary X-ray studies of oligandrin, a sterol-carrier elicitor from Pythium oligandrumM.-B. Lascombe, M.-L. Milat, J.-P. Blein, F. Panabières, M. Ponchet and T. PrangéSynopsis: Oligandrin, a small 10 kDa phytotoxin with sterol-carrier properties, has been crystallized from PEG 4000 at pH 4.5. Online November 2000 |
Acta Cryst. (2000). D56, 1501-1504 [ doi:10.1107/S0907444900010040 ] The purification, crystallization and preliminary structural characterization of glucose-1-phosphate thymidylyltransferase (RmlA), the first enzyme of the dTDP-L-rhamnose synthesis pathway from Pseudomonas aeruginosaW. Blankenfeldt, M.-F. Giraud, G. Leonard, R. Rahim, C. Creuzenet, J. S. Lam and J. H. NaismithSynopsis: The anabolism of L-rhamnose in many pathogenic bacteria presents itself as a possible novel therapeutic target. RmlA is the first of the four enzymes involved in this pathway. Crystallization and preliminary structural characterization are reported. Online November 2000 |
Acta Cryst. (2000). D56, 1505-1507 [ doi:10.1107/S0907444900010076 ] Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genomeD. Borek and M. JaskólskiSynopsis: A new E. coli L-asparaginase belonging to the class of Ntn hydrolases has been crystallized in the orthorhombic space group P212121. The crystals diffract to 1.65 Å resolution and contain an ( Online November 2000 |
Acta Cryst. (2000). D56, 1508-1509 [ doi:10.1107/S0907444900011756 ] Purification, crystallization and preliminary diffraction study of
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Acta Cryst. (2000). D56, 1510-1511 [ doi:10.1107/S0907444900010751 ] Apotheosis, not apocalypse: methods in protein crystallographyV. S. Lamzin, A. Perrakis, G. Bricogne, J. Jiang, S. Swaminathan and J. L. SussmanSynopsis: Report of the workshop Toward Automation of Structure Determination in Macromolecular Crystallography held on 20-21 June 1999. Online November 2000 |
Acta Cryst. (2000). D56, 1512 [ doi:10.1107/S0907444900013640 ] Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase from Corynrbacterium glutamicum. ErratumG. F. Audette, J. W. Quail, K. Hayakawa, C. Bai, R. Chen and L. T. J. DelbaereSynopsis: An erratum to Acta Cryst. (1999), D55, 1584-1585. Online November 2000 |
Acta Cryst. (2000). D56, 1512 [ doi:10.1107/S0907444900014219 ] Crystallization and preliminary X-ray analysis of the conserved domain IV of Escherichia coli 4.5S RNA. ErratumL. Jovine, T. Hainzl, C. Oubridge and K. NagaiSynopsis: An erratum to Acta Cryst. (2000), D56, 1033-1037. Online November 2000 |
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