(IUCr) Contents for Acta Crystallographica Section D Vol. 54 Part 5 (September 1998)

Acta Cryst. (1998). D54, 711-717 [ doi:10.1107/S0907444997010457 ]

Structure of 3,4-Dichloroisocoumarin-Inhibited Factor D

L. B. Cole, J. M. Kilpatrick, N. Chu and Y. S. Babu

Synopsis: The structure of the enzyme:inhibitor covalent adduct of factor D with 3,4-dichloroisocoumarin to a resolution of 1.8 Å is described. This represents the first structural analysis of factor D with a mechanism-based inhibitor.

Online September 1998

Acta Cryst. (1998). D54, 718-725 [ doi:10.1107/S0907444997012481 ]

Integrated Software for a Macromolecular Crystallography Synchrotron Beamline

J. M. Skinner and R. M. Sweet

Synopsis: Users of beamline X12-C at the National Synchrotron Light Source communicate with all the experimental apparatus, including both the data-collection equipment and the beamline components, through an easy-to-use graphical user interface (GUI). Important features of the system are modularity, ease of use, and automatic logging of experimental operations and parameters to facilitate nearly automatic data reduction.

Online September 1998

Acta Cryst. (1998). D54, 726-734 [ doi:10.1107/S0907444997012456 ]

On the Ab Initio Solution of the Phase Problem for Macromolecules at Very Low Resolution. II. Generalized Likelihood Based Approach to Cluster Discrimination

V. Y. Lunin, N. L. Lunina, T. E. Petrova, A. G. Urzhumtsev and A. D. Podjarny

Synopsis: A straightforward computer procedure is suggested to choose between several alternative solutions of the low-resolution phase problem.

Online September 1998

Acta Cryst. (1998). D54, 735-749 [ doi:10.1107/S0907444997016223 ]

The Refined Structure of dUTPase from Escherichia coli

Z. Dauter, K. S. Wilson, G. Larsson, P. O. Nyman and E. S. Cedergren-Zeppezauer

Synopsis: A detailed description of the refined structure of E. coli dUTPase at 1.9 Å resolution shows a fold similar to other known structures of trimeric dUTPases, with a highly intertwined architecture and a disordered C-terminal arm. The use of optimized anomalous scattering measurements for the two heavy-atom derivatives led to a high quality initial electron-density map.

Online September 1998

Acta Cryst. (1998). D54, 750-756 [ doi:10.1107/S0907444997016247 ]

Modified Phased Translation Functions and their Application to Molecular-Fragment Location

K. Cowtan

Synopsis: A modified phased translation function is applied to the location of small molecular fragments in noisy electron-density maps. Reciprocal-space implementation leads to speed improvements and some improved discrimination over real-space approaches.

Online September 1998

Acta Cryst. (1998). D54, 757-766 [ doi:10.1107/S0907444997016806 ]

Structure of the C-Type Lectin Carbohydrate Recognition Domain of Human Tetranectin

J. S. Kastrup, B. B. Nielsen, H. Rasmussen, T. L. Holtet, J. H. Graversen, M. Etzerodt, H. C. Thøgersen and I. K. Larsen

Synopsis: The crystal structure has been determined at 2.0 Å resolution and detailed information on the two calcium binding sites has been obtained. This is essential for the elucidation of the specificity of tetranectin towards oligosaccharides.

Online September 1998

Acta Cryst. (1998). D54, 767-779 [ doi:10.1107/S0907444997016922 ]

Structures of Monoclinic Lysozyme Iodide at 1.6 Å and of Triclinic Lysozyme Nitrate at 1.1 Å

L. K. Steinrauf

Synopsis: Ultra high resolution structures of lysozyme reveal the variable nature of anion sites.

Online September 1998

Acta Cryst. (1998). D54, 780-798 [ doi:10.1107/S0907444997018611 ]

Structure of a Non-psychrophilic Trypsin from a Cold-Adapted Fish Species

H. K. Schrøder, N. P. Willassen and A. O. Smalås

Synopsis: The 1.7 Å crystal structure of the non-psychrophidic cationic salmon trypsin comprise 4 molecules per asymmetric unit. The four independently refined molecules are compared to each other to the cold-adapted anionic salmon trypsin and the bovine trypsin, to search for the structural basis of the psychrophilic trypsin

Online September 1998

Acta Cryst. (1998). D54, 799-804 [ doi:10.1107/S0907444997018805 ]

The Use of SnB to Determine an Anomalous Scattering Substructure

G. D. Smith, B. Nagar, J. M. Rini, H. A. Hauptman and R. H. Blessing

Synopsis: A method is described for the determination of an anomalous scattering substructure using data at a single wavelength and the direct-methods program SnB.

Online September 1998

Acta Cryst. (1998). D54, 805-816 [ doi:10.1107/S0907444997018878 ]

Structure of Bacteriophage T4 Fibritin M: a Troublesome Packing Arrangement

S. V. Strelkov, Y. Tao, M. M. Shneider, V. V. Mesyanzhinov and M. G. Rossmann

Synopsis: The crystal structure of a fragment of fibritin, a predominantly coiled-coil structural protein from bacteriophage, has been determined to 1.85 Å resolution. Careful analysis of partial disorder associated with the crystal packing arrangement in the unusual space group P3 and appropriate modeling of the solvent structure were necessary for achieving good crystallographic refinement.

Online September 1998

Acta Cryst. (1998). D54, 817-821 [ doi:10.1107/S0907444997019434 ]

On the Use of Strong Patterson Function Signals in Many-Body Molecular Replacement

J. Navaza, E. H. Panepucci and C. Martin

Synopsis: Strong information from self-rotation and Patterson functions is used to reduce the number of independent molecules to locate by molecular-replacement techniques.

Online September 1998

Acta Cryst. (1998). D54, 822-827 [ doi:10.1107/S0907444997020064 ]

Detection and Use of Pseudo-Translation in Determination of Protein Structures

Y. M. Chook, W. N. Lipscomb and H. Ke

Synopsis: Pseudo-translation symmetry in protein crystals of cyclophilin C and chorismate mutase and its use in structure determination is described.

Online September 1998

Acta Cryst. (1998). D54, 828-833 [ doi:10.1107/S0907444997020349 ]

STEP - a Trial-and-Error Procedure for Crystal Structure Determination. II. The Determination of Two Small Protein Structures

L. Lipu, J. Jian, X. Xiaofeng and Y. Yonggeng

Synopsis: This paper descibes the difficulties in the process of using the trial-and-error SYSTEM90 program to determine ab initio the structures of two small proteins App and rubredoxin with high-resolution data. Strategies to overcome the difficulties are discussed and the upgraded SYSTEM95 program was used successfully.

Online September 1998

Acta Cryst. (1998). D54, 834-843 [ doi:10.1107/S090744499800122X ]

X-ray Structure of Human Lysozyme Labelled with 2',3'-Epoxypropyl -Glycoside of Man-1,4-GlcNAc. Structural Change and Recognition Specificity at Subsite B

M. Muraki, K. Harata, N. Sugita and K. Sato

Synopsis: The X-ray structure of human lysozyme labelled with the 2',3'-epoxypropyl [beta] -glycoside of Man- [beta] 1,4-GlcNAc was determined by molecular replacement and refined to an R value of 0.168 at 2.1 Å resolution. Cell dimensions were a = 36.39, b = 116.38 and c = 30.91 Å (space group: P2₁2₁2₁). The result explained the difference in molecular packing compared with wild-type human lysozyme and the origin of carbohydrate-residue recognition specificity at subsite B.

Online September 1998

Acta Cryst. (1998). D54, 844-847 [ doi:10.1107/S0907444998001218 ]

Quaternary Structure of UEA-II, the Chitobiose Specific Lectin from Gorse

M.-H. Dao-Thi, P. Rizkallah, L. Wyns, F. Poortmans and R. Loris

Synopsis: The chitobiose specific Ulex europaeus lectin II crystallizes in space group P3₂21 with unit-cell dimensions a = b = 105.54, c = 176.26 Å. The lectin forms a tetramer similar, but not identical to the PHA-L tetramer.

Online September 1998

Acta Cryst. (1998). D54, 848-853 [ doi:10.1107/S0907444998001875 ]

A Description of Imperfections in Protein Crystals

C. Nave

Synopsis: A three-parameter model is derived to describe the imperfections of protein crystals and their effect on rocking widths and diffracted-beam divergences. Measurements of frozen lysozyme crystals are presented in order to illustrate how the parameters describing crystal imperfection can be estimated.

Online September 1998

Acta Cryst. (1998). D54, 854-866 [ doi:10.1107/S0907444998002005 ]

Structure of Glucoamylase from Saccharomycopsis fibuligera at 1.7 Å Resolution

J. Sevcík, A. Solovicová, E. Hostinová, J. Gasperík, K. S. Wilson and Z. Dauter

Synopsis: The structure of glucoamylase from S. fibuligera has been solved at 1.7 Å resolution. Refinement from the initial molecular-replacement model involved the unrestrained automated refinement procedure (uARP) combined with the maximum-likelihood refinement program REFMAC. This is the first report of the three-dimensional structure of a yeast family 15 glucoamylase.

Online September 1998

Acta Cryst. (1998). D54, 867-872 [ doi:10.1107/S0907444998002297 ]

Nucleation in Protein Crystallization

J. Drenth and C. Haas

Synopsis: The growth of high-concentration fluctuations leads to phase separation and nucleation in supersaturated protein solutions. From NMR measurements of the induction time before crystallization, it can be concluded that the crystallization of lysozyme is a transient process and not a steady-state process.

Online September 1998

Acta Cryst. (1998). D54, 873-877 [ doi:10.1107/S0907444998002455 ]

Accessing Lysozyme Nucleation with a Novel Dynamic Light Scattering Detector

R. Peters, Y. Georgalis and W. Saenger

Synopsis: A novel fiber-optic backscattering detector was employed to investigate nucleation in lysozyme solutions. The time evolution of the observed clusters can be employed in diagnosing conditions that favor protein crystallization.

Online September 1998

Acta Cryst. (1998). D54, 878-890 [ doi:10.1107/S0907444998002467 ]

Structure Determination of the $\boldvarphi$ X174 Closed Procapsid

T. Dokland, R. McKenna, D. M. Sherman, B. R. Bowman, W. F. Bean and M. G. Rossmann

Synopsis: The structure of the closed procapsid of the single-stranded DNA bacteriophage [varphi] X174 was determined to 3.5 Å resolution by molecular-replacement real-space averaging starting from a very poor model based on an electron microscopic reconstruction. Electron microscopy of thin-sectioned crystals was used to aid in the interpretation of the packing arrangement.

Online September 1998

Acta Cryst. (1998). D54, 891-898 [ doi:10.1107/S0907444998002480 ]

Structure of Ubiquitin-Conjugating Enzyme 9 Displays Significant Differences with Other Ubiquitin-Conjugating Enzymes Which May Reflect its Specificity for Sumo Rather Than Ubiquitin

M. F. Giraud, J. M. P. Desterro and J. H. Naismith

Synopsis: The structure of Ubc9, a sumo-conjugating enzyme, has been determined by molecular replacement to 2.8 Å resolution. The structure suggests how Ubc9 conjugates sumo rather than ubiquitin.

Online September 1998

Acta Cryst. (1998). D54, 899-904 [ doi:10.1107/S0907444998002844 ]

Locations of Bromide Ions in Tetragonal Lysozyme Crystals

K. Lim, A. Nadarajah, E. L. Forsythe and M. L. Pusey

Synopsis: Using a difference Fourier map between tetragonal lysozyme bromide and chloride, five possible anion-binding sites have been identified.

Online September 1998

Acta Cryst. (1998). D54, 905-921 [ doi:10.1107/S0907444998003254 ]

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

A. T. Brünger, P. D. Adams, G. M. Clore, W. L. DeLano, P. Gros, R. W. Grosse-Kunstleve, J.-S. Jiang, J. Kuszewski, M. Nilges, N. S. Pannu, R. J. Read, L. M. Rice, T. Simonson and G. L. Warren

Synopsis: A new software system for macromolecular structure determination is presented. The program covers nearly all aspects of macromolecular structure determination by X-ray crystallography and solution NMR.

Online September 1998

Acta Cryst. (1998). D54, 922-937 [ doi:10.1107/S090744499800376X ]

X-ray Topographic Studies of Protein Crystal Perfection and Growth

I. Dobrianov, K. D. Finkelstein, S. G. Lemay and R. E. Thorne

Synopsis: X-ray topography and mosaicity measurements show that variations in solution conditions during protein crystal growth (an important feature of vapor diffusion and other popular growth methods) can produce crystal disorder. Several mechanisms may contribute to the observed disorder. These methods provide a very useful probe of protein crystal perfection and have been used to characterize the effects of variations in solution conditions during crystal growth on protein crystal perefection.

Online September 1998

Acta Cryst. (1998). D54, 938-953 [ doi:10.1107/S0907444998004284 ]

Continuous and Discontinuous Changes in the Unit Cell of HIV-1 Reverse Transcriptase Crystals on Dehydration

R. M. Esnouf, J. Ren, E. F. Garman, D. O. Somers, C. K. Ross, E. Y. Jones, D. K. Stammers and D. I. Stuart

Synopsis: A crystal form of HIV-1 reverse transcriptase complexed to inhibitors which normally diffracts to 3.7 Å can be subjected to controlled dehydration to increase the diffraction limit to 2.2 Å. A range of different crystal forms have been identified and analysed, giving insight into the flexibility of this therapeutically important enzyme.

Online September 1998

Acta Cryst. (1998). D54, 954-963 [ doi:10.1107/S0907444998004429 ]

Recognition of RNase Sa by the Inhibitor Barstar: Structure of the Complex at 1.7 Å Resolution

J. Sevcík, L. Urbanikova, Z. Dauter and K. S. Wilson

Synopsis: The structure of Ribonuclease Sa from Streptomyces aureofaciens has been solved in complex with the inhibitor barstar at 1.7 Å resolution. The nature of the interface of the complex is discussed and compared to that of the natural barnase-barstar system.

Online September 1998

Acta Cryst. (1998). D54, 964-974 [ doi:10.1107/S0907444998005125 ]

Structure of Dimeric and Monomeric Erabutoxin a Refined at 1.5 Å Resolution

V. Nastopoulos, P. N. Kanellopoulos and D. Tsernoglou

Synopsis: High-resolution X-ray data to 1.5 Å have been used to refine the crystal structures of dimeric and monomeric erabutoxin a. Significant protein discrete disorder and solvent order is described.

Online September 1998

crystallization papers

Acta Cryst. (1998). D54, 975-981 [ doi:10.1107/S0907444997011554 ]

Crystallization of CcdB

M. H. Dao-Thi, L. Wyns, F. Poortmans, E. M. Bahassi, M. Couturier and R. Loris

Synopsis: The crystallization behavior of CcdB was investigated in detail. A novel crystal form, diffracting to 1.5 Å, proved to be suitable for structure determination.

Online September 1998

Acta Cryst. (1998). D54, 982-985 [ doi:10.1107/S090744499800033X ]

Crystallization and preliminary X-ray analysis of pig E3, lipoamide dehydrogenase

T. Toyoda, R. Kobayashi, T. Sekiguchi, K. Koike, M. Koike and A. Takenaka

Synopsis: Pig heart lipoamide dehydrogenase was crystallized and preliminarily X-ray analyzed by molecular replacement method.

Online September 1998

Acta Cryst. (1998). D54, 986-988 [ doi:10.1107/S0907444998000353 ]

Purification, crystallization and preliminary X-ray crystallographic analysis of Pyrococcus furiosus DNA polymerase

S. Goldman, R. Kim, L. W. Hung, J. Jancarik and S. H. Kim

Synopsis: Crystallization of DNA polymerase from the hyperthermophilic Archaeon Pyrococcus furiosus.

Online September 1998

Acta Cryst. (1998). D54, 989-990 [ doi:10.1107/S0907444998000985 ]

Purification, crystallization and preliminary crystallographic analysis of bovine cytosolic brain-type creatine kinase

A. Loew and B. Bax

Synopsis: Bovine cytosolic brain-type creatine kinase hasd been crystallized. Diffraction data have been collected to 2.7 Å.

Online September 1998

Acta Cryst. (1998). D54, 991-993 [ doi:10.1107/S0907444998001048 ]

Crystallization and preliminary X-ray crystallographic studies of the plant aspartic proteinase cardosin A

I. Bento, C. Frazão, R. Coelho, K. Wilson, Z. Dauter and M. A. Carrondo

Synopsis: Crystallization and preliminary crystal analysis of cardosina, an aspartic proteinase found in flowers of the plant Cynara Cardunculus.

Online September 1998

Acta Cryst. (1998). D54, 994-995 [ doi:10.1107/S0907444998001553 ]

Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon

M. Zhou, C. Mao, A. C. Rodriguez, J. R. Kiefer, R. B. Kucera and L. S. Beese

Synopsis: The hyperthermostable DNA polymerase (polymerase B family) from a marine Thermococcus archaeon has been crystallized, and a complete dataset was collected to 2.2 Å resolution. The structure of this enzyme will provide the first structural data on the archaeal and hyperthermostable classes of DNA polymerases.

Online September 1998

Acta Cryst. (1998). D54, 996-998 [ doi:10.1107/S0907444998001887 ]

Crystallization and preliminary X-ray analysis of Escherichia coli GlnK

K. H. R. Macpherson, Y. Xu, E. Cheah, P. D. Carr, W. C. van Heeswijk, H. V. Westerhoff, E. Luque, S. G. Vasudevan and D. L. Ollis

Synopsis: The expression, purification, crystallization and preliminary X-ray characterization of the GlnK protein is described. Crystallization and preliminary X-ray characterization of the protein complexed with ATP is also described.

Online September 1998

Acta Cryst. (1998). D54, 999-1001 [ doi:10.1107/S0907444998001851 ]

Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain

M. Degenhardt, W. Weber, S. Eschenburg, K. Dierks, S. S. Funari, G. Rapp and C. Betzel

Synopsis: Crystallization of the hydrophilic ectodomain of the epidermal growth factor (EGF) receptor and low resolution X-ray stdies in combination with small angle X-ray diffraction and dynamic light-scattering techniques.

Online September 1998

Acta Cryst. (1998). D54, 1002-1004 [ doi:10.1107/S0907444998002443 ]

Crystallization and preliminary X-ray diffraction studies of DNA polymerase from the thermophilic archaeon Sulfolobus solfataricus

V. Nastopoulos, F. M. Pisani, C. Savino, L. Federici, M. Rossi and D. Tsernoglou

Synopsis: The thermophilic and thermostable family B DNA polymerase from the archaeon Sulfolobus solfataricus has been crystallized in the C2 space group with cell dimensions a = 187.4, b = 68.5, c = 125.8 Å and [beta] = 107.8°. Crystals diffract up to 2.7 Å resolution.

Online September 1998

Acta Cryst. (1998). D54, 1005-1007 [ doi:10.1107/S0907444998002479 ]

Crystallization and preliminary X-ray diffraction analysis of antigen-binding fragments which are specific for antigenic conformations of sialic acid homopolymers

S. I. Patenaude, S. M. Vijay, Q. L. Yang, H. J. Jennings and S. V. Evans

Synopsis: The antigen-binding fragments (Fab) of one protective (13D9) and one non-protective (6B9) monoclonal antibody specific for the capsular polysaccharides of group B meningococci have been crystallized and undergone preliminary X-ray diffraction analysis. This is hoped to aid in the production of a vaccine for the disease meningococcal meningitis.

Online September 1998

Acta Cryst. (1998). D54, 1008-1011 [ doi:10.1107/S0907444998002571 ]

Crystallization and preliminary X-ray crystallographic studies of the 13-fold symmetric portal protein of bacteriophage SPP1

P. Jekow, S. Schaper, D. Günther, P. Tavares and W. Hinrichs

Synopsis: Portal proteins are essential in bacteriophage morphogenesis. Preliminary diffraction data of the crystallized portal protein gp6 from bacteriophage SPP1 confirmed its 13-fold symmetry.

Online September 1998

Acta Cryst. (1998). D54, 1012-1013 [ doi:10.1107/S0907444998002583 ]

Preliminary crystallographic studies of citrate synthase from an Antarctic psychrotolerant bacterium

U. Gerike, R. J. M. Russell, M. J. Danson, N. J. Russell, D. W. Hough and G. L. Taylor

Synopsis: Recombinant citrate synthase from a psychrotolerant bacterium, DS2-3R, recently isolated in Antarctica, has been crystallized. The crystals belong to space group P6₁22 or P6₅22, with cell dimensions a = b = 70.8, c = 307.8 Å. Knowledge of the structure of this enzyme will add to the understanding of cold activity and thermolability, and will be of biotechnological interest.

Online September 1998

Acta Cryst. (1998). D54, 1014-1016 [ doi:10.1107/S0907444998003266 ]

Crystallographic characterization of Pap1-DNA complex

Y. Fujii, T. Ohira, Y. Kyougoku, T. Toda, M. Yanagida and T. Hakoshima

Synopsis: Pap1 is a fission yeast bZIP transcription factor that binds to non-consensus DNA sequences, TTACGTAA and TTAGTCA. Highly ordered crystals of Pap1-DNA complex that diffract up to 2.0 Å resolution have been obtained.

Online September 1998

Acta Cryst. (1998). D54, 1017-1019 [ doi:10.1107/S0907444998003448 ]

Crystallization and preliminary X-ray diffraction studies on the water soluble form of rat heme oxygenase-1 in complex with heme

Y. Omata, S. Asada, H. Sakamoto, K. Fukuyama and M. Noguchi

Synopsis: The water-soluble portion of rat heme oxygenase-1 has been expressed in E. coli and crystallized in the form of a complex with heme. The crystals belong to space group P4₁2₁2 or P4₃2₁2 and diffracted to better than 3.0 Å resolution.

Online September 1998

Acta Cryst. (1998). D54, 1020-1022 [ doi:10.1107/S0907444998003497 ]

Crystallization and preliminary X-ray analysis of the -isoform of glutamate decarboxylase from Escherichia coli

V. N. Malashkevich, D. De Biase, Z. Markovic-Housley, M. P. Schlunegger, F. Bossa and J. N. Jansonius

Synopsis: Escherichia coli glutamate decarboxylase [alpha] and [beta] have been expressed separately. Crystals of the latter (space group P3₁ or P3₂) have been used for a preliminary X-ray analysis at 2.5 Å resolution.

Online September 1998

Acta Cryst. (1998). D54, 1023-1025 [ doi:10.1107/S0907444998003965 ]

Crystallization of succinylated concanavalin A bound to a synthetic bivalent ligand and preliminary structural analysis

D. N. Moothoo, S. A. McMahon, S. M. Dimick, E. J. Toone and J. H. Naismith

Synopsis: The article describes the first crystallization of a lectin bound to a synthetic multivalent ligand. Despite solution evidence that the protein is dimeric, a regular concanavalin A tetramer is found in the crystal with extensive contacts holding it together.

Online September 1998

Acta Cryst. (1998). D54, 1026-1029 [ doi:10.1107/S0907444998004132 ]

Crystallization and preliminary X-ray diffraction studies of the heterogeneously glycosylated enzyme rhamnogalacturonan acetylesterase from Aspergillus aculeatus

A. Mølgaard, J. F. W. Petersen, S. Kauppinen, H. Dalbøge, A. H. Johnsen, J.-C. Navarro Poulsen and S. Larsen

Synopsis: Rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been crystallized in three different polymorphic modifications. Mass spectra showed that the ability to crystallize depends on the protein samples' degree of glycosylation. Native data sets have been collected to 1.55 Å for the orthorhombic and to 2.5 Å for the trigonal form.

Online September 1998

Acta Cryst. (1998). D54, 1030-1031 [ doi:10.1107/S0907444998004272 ]

Purification, crystallization and preliminary X-ray analysis of human recombinant cytosolic serine hydroxymethyltransferase

S. B. Renwick, J. V. Skelly, K. J. Chave, P. G. Sanders, K. Snell and U. Baumann

Synopsis: Human serine hydroxymethlytransferase, a key enzyme in C1 metabolism and attractive anti-cancer target, has been overexpressed and successfully crystallized. The crystals diffract to at least 3 Å resolution and structure determination is under way.

Online September 1998

Acta Cryst. (1998). D54, 1032-1034 [ doi:10.1107/S090744499800434X ]

Crystallization and preliminary X-ray characterization of aspartate aminotransferase from an extreme thermophile, Thermus thermophilus HB8

T. Nakai, K. Okada, S. Kawaguchi, R. Kato, S. Kuramitsu and K. Hirotsu

Synopsis: Recombinant aspartate aminotransferase from an extreme thermophile has been crystallized in two different crystal forms. One form contains one dimer per asymmetric unit and diffracts to 2.1 Å resolution, while the other form contains two dimers and diffracts to 2.5 Å.

Online September 1998

Acta Cryst. (1998). D54, 1035-1038 [ doi:10.1107/S0907444998004946 ]

Crystallization and preliminary X-ray diffraction studies of the oxygenating subunit of 3,6-diketocamphane monooxygenase from Pseudomonas putida

E. J. McGhie, M. N. Isupov, E. Schröder and J. A. Littlechild

Synopsis: Crystals of the oxygenating subunit of 3,6-diketocamphane monooxygenase from Pseudomonas putida have been obtained using two different conditions.

Online September 1998

short communications

Acta Cryst. (1998). D54, 1039-1042 [ doi:10.1107/S0907444997020210 ]

Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium

R. Reitzer, M. Krasser, G. Jogl, W. Buckel, H. Bothe and C. Kratky

Synopsis: Glutamate mutase was reconstituted with aquo- and cyanotobalamin, yielding inactive but stable enzyme, which was crystallized. One of its components was separately complexed with cofactor and crystallized.

Online September 1998

Acta Cryst. (1998). D54, 1043-1045 [ doi:10.1107/S0907444998000341 ]

Cloning, overproduction, purification and crystallization of the DNA binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima

E. Christodoulou and C. E. Vorgias

Synopsis: The thermostable DNA binding protein HU from Thermotoga maritima has been purified and crystallized. A preliminary X-ray diffraction analysis has been reported.

Online September 1998

Acta Cryst. (1998). D54, 1046-1048 [ doi:10.1107/S0907444998001607 ]

Expression, purification, crystallization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei

M. H. Dao-Thi, T. R. Transue, R. Pellé, N. B. Murphy, F. Poortmans and J. Steyaert

Synopsis: Cycophilin A from the bovine parasite Trypanosoma brucei brucei had been cloned, expressed, purified and crystallized in the presence of cyclosporin A. The orthorombic crystals diffract to better than 2.1 Å.

Online September 1998

Acta Cryst. (1998). D54, 1049-1052 [ doi:10.1107/S0907444998002303 ]

Structure of pig plasma retinol-binding protein at 1.65 Å resolution

G. Zanotti, M. Panzalorto, A. Marcato, G. Malpeli, C. Folli and R. Berni

Synopsis: The structure of an orthorhombic crystal form of pig plasma retinol-binding protein (RBP) has been determined at 1.65 Å resolution. New structural details in regard to the interaction of retinol with RBP and to the role of Cd²⁺ in promoting RBP crystallization are described.

Online September 1998

Acta Cryst. (1998). D54, 1053-1060 [ doi:10.1107/S0907444998003588 ]

Rapid X-ray diffraction analysis of HIV-1 protease-inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme

S. Munshi, Z. Chen, Y. Li, D. B. Olsen, M. E. Fraley, R. W. Hungate and L. C. Kuo

Synopsis: A weakly bound inhibitor in the crystals of HIV-1 protease-inhibitor complex can be replaced by a more potent inhibitor. Structure of the resulting complex is similar to that obtained with the co-crystals of HIV-1 protease and the potent inhibitor.

Online September 1998

Acta Cryst. (1998). D54, 1061-1063 [ doi:10.1107/S0907444998004120 ]

Crystallization and preliminary X-ray studies of purine nucleoside phosphorylase from Cellulomonas sp.

A. Bzowska, J. Tebbe, M. Luic, B. Wielgus-Kutrowska, W. Schröder, D. Shugar, W. Saenger and G. Koellner

Synopsis: Preliminary X-ray studies of two crystal forms of PNP from Cellulomonas sp.

Online September 1998


	Cover illustration: The balhimycin dimer, with citrate and acetate ions in the binding pockets, colour coded on a scale where the most mobile atoms are red and the least mobile are blue. The binding pockets are clearly the most mobile, consistent with the idea that they can open and close to complex with cell-wall binding peptides. Courtesy of George Sheldrick.

Acta Crystallographica Section D

Biological Crystallography

Volume 54, Part 5 (September 1998)

research papers

Structure of 3,4-Dichloroisocoumarin-Inhibited Factor D

L. B. Cole, J. M. Kilpatrick, N. Chu and Y. S. Babu

Integrated Software for a Macromolecular Crystallography Synchrotron Beamline

J. M. Skinner and R. M. Sweet

On the Ab Initio Solution of the Phase Problem for Macromolecules at Very Low Resolution. II. Generalized Likelihood Based Approach to Cluster Discrimination

V. Y. Lunin, N. L. Lunina, T. E. Petrova, A. G. Urzhumtsev and A. D. Podjarny

The Refined Structure of dUTPase from Escherichia coli

Z. Dauter, K. S. Wilson, G. Larsson, P. O. Nyman and E. S. Cedergren-Zeppezauer

Modified Phased Translation Functions and their Application to Molecular-Fragment Location

K. Cowtan

Structure of the C-Type Lectin Carbohydrate Recognition Domain of Human Tetranectin

J. S. Kastrup, B. B. Nielsen, H. Rasmussen, T. L. Holtet, J. H. Graversen, M. Etzerodt, H. C. Thøgersen and I. K. Larsen

Structures of Monoclinic Lysozyme Iodide at 1.6 Å and of Triclinic Lysozyme Nitrate at 1.1 Å

L. K. Steinrauf

Structure of a Non-psychrophilic Trypsin from a Cold-Adapted Fish Species

H. K. Schrøder, N. P. Willassen and A. O. Smalås

The Use of SnB to Determine an Anomalous Scattering Substructure

G. D. Smith, B. Nagar, J. M. Rini, H. A. Hauptman and R. H. Blessing

Structure of Bacteriophage T4 Fibritin M: a Troublesome Packing Arrangement

S. V. Strelkov, Y. Tao, M. M. Shneider, V. V. Mesyanzhinov and M. G. Rossmann

On the Use of Strong Patterson Function Signals in Many-Body Molecular Replacement

J. Navaza, E. H. Panepucci and C. Martin

Detection and Use of Pseudo-Translation in Determination of Protein Structures

Y. M. Chook, W. N. Lipscomb and H. Ke

STEP - a Trial-and-Error Procedure for Crystal Structure Determination. II. The Determination of Two Small Protein Structures

L. Lipu, J. Jian, X. Xiaofeng and Y. Yonggeng

X-ray Structure of Human Lysozyme Labelled with 2',3'-Epoxypropyl -Glycoside of Man-1,4-GlcNAc. Structural Change and Recognition Specificity at Subsite B

M. Muraki, K. Harata, N. Sugita and K. Sato

Quaternary Structure of UEA-II, the Chitobiose Specific Lectin from Gorse

M.-H. Dao-Thi, P. Rizkallah, L. Wyns, F. Poortmans and R. Loris

A Description of Imperfections in Protein Crystals

C. Nave

Structure of Glucoamylase from Saccharomycopsis fibuligera at 1.7 Å Resolution

J. Sevcík, A. Solovicová, E. Hostinová, J. Gasperík, K. S. Wilson and Z. Dauter

Nucleation in Protein Crystallization

J. Drenth and C. Haas

Accessing Lysozyme Nucleation with a Novel Dynamic Light Scattering Detector

R. Peters, Y. Georgalis and W. Saenger

Structure Determination of the X174 Closed Procapsid

T. Dokland, R. McKenna, D. M. Sherman, B. R. Bowman, W. F. Bean and M. G. Rossmann

Structure of Ubiquitin-Conjugating Enzyme 9 Displays Significant Differences with Other Ubiquitin-Conjugating Enzymes Which May Reflect its Specificity for Sumo Rather Than Ubiquitin

M. F. Giraud, J. M. P. Desterro and J. H. Naismith

Locations of Bromide Ions in Tetragonal Lysozyme Crystals

K. Lim, A. Nadarajah, E. L. Forsythe and M. L. Pusey

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

A. T. Brünger, P. D. Adams, G. M. Clore, W. L. DeLano, P. Gros, R. W. Grosse-Kunstleve, J.-S. Jiang, J. Kuszewski, M. Nilges, N. S. Pannu, R. J. Read, L. M. Rice, T. Simonson and G. L. Warren

X-ray Topographic Studies of Protein Crystal Perfection and Growth

I. Dobrianov, K. D. Finkelstein, S. G. Lemay and R. E. Thorne

Continuous and Discontinuous Changes in the Unit Cell of HIV-1 Reverse Transcriptase Crystals on Dehydration

R. M. Esnouf, J. Ren, E. F. Garman, D. O. Somers, C. K. Ross, E. Y. Jones, D. K. Stammers and D. I. Stuart

Recognition of RNase Sa by the Inhibitor Barstar: Structure of the Complex at 1.7 Å Resolution

J. Sevcík, L. Urbanikova, Z. Dauter and K. S. Wilson

Structure of Dimeric and Monomeric Erabutoxin a Refined at 1.5 Å Resolution

V. Nastopoulos, P. N. Kanellopoulos and D. Tsernoglou

crystallization papers

Crystallization of CcdB

M. H. Dao-Thi, L. Wyns, F. Poortmans, E. M. Bahassi, M. Couturier and R. Loris

Crystallization and preliminary X-ray analysis of pig E3, lipoamide dehydrogenase

T. Toyoda, R. Kobayashi, T. Sekiguchi, K. Koike, M. Koike and A. Takenaka

Purification, crystallization and preliminary X-ray crystallographic analysis of Pyrococcus furiosus DNA polymerase

S. Goldman, R. Kim, L. W. Hung, J. Jancarik and S. H. Kim

Purification, crystallization and preliminary crystallographic analysis of bovine cytosolic brain-type creatine kinase

A. Loew and B. Bax

Crystallization and preliminary X-ray crystallographic studies of the plant aspartic proteinase cardosin A

I. Bento, C. Frazão, R. Coelho, K. Wilson, Z. Dauter and M. A. Carrondo

Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon

M. Zhou, C. Mao, A. C. Rodriguez, J. R. Kiefer, R. B. Kucera and L. S. Beese

Crystallization and preliminary X-ray analysis of Escherichia coli GlnK

K. H. R. Macpherson, Y. Xu, E. Cheah, P. D. Carr, W. C. van Heeswijk, H. V. Westerhoff, E. Luque, S. G. Vasudevan and D. L. Ollis

Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain

M. Degenhardt, W. Weber, S. Eschenburg, K. Dierks, S. S. Funari, G. Rapp and C. Betzel

Crystallization and preliminary X-ray diffraction studies of DNA polymerase from the thermophilic archaeon Sulfolobus solfataricus

V. Nastopoulos, F. M. Pisani, C. Savino, L. Federici, M. Rossi and D. Tsernoglou

Crystallization and preliminary X-ray diffraction analysis of antigen-binding fragments which are specific for antigenic conformations of sialic acid homopolymers

S. I. Patenaude, S. M. Vijay, Q. L. Yang, H. J. Jennings and S. V. Evans

Crystallization and preliminary X-ray crystallographic studies of the 13-fold symmetric portal protein of bacteriophage SPP1

Structure Determination of the $\boldvarphi$ X174 Closed Procapsid