Acta Crystallographica Section D

Biological Crystallography

Volume 54, Part 4 (July 1998)



[Issue Author Index][Volume Author Index]
[Cover illustration] 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.

research papers


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Acta Cryst. (1998). D54, 481-486  [ doi:10.1107/S090744499701216X ]

Structure of Sulfur-Substituted Rhodanese at 1.36 Å Resolution

F. Gliubich, R. Berni, M. Colapietro, L. Barba and G. Zanotti

Synopsis: X-ray diffraction data for the enzyme bovine liver rhodanese have been recorded at 100 K and the crystal structure has been refined anisotropically at 1.36 Å resolution. Details of the crystal structure and of the active site are described.

Online July 1998


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Acta Cryst. (1998). D54, 487-493  [ doi:10.1107/S0907444997011980 ]

Miscellaneous Algorithms for Density Modification

K. Cowtan and P. Main

Synopsis: Efficient algorithms are described for data scaling, map interpolation, automatic averaging mask calculation and averaging operator refinement, for use in density-modification calculations and elsewhere. These algorithms have contributed significantly to the speed and automation achieved in the dm software package.

Online July 1998


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Acta Cryst. (1998). D54, 494-500  [ doi:10.1107/S0907444997012225 ]

Structure of an Enantiomeric Protein, D-Monellin at 1.8 Å Resolution

L.-W. Hung, M. Kohmura, Y. Ariyoshi and S.-H. Kim

Synopsis: Two crystal forms of D-monellin, the enantiomer of a natural sweet protein monellin, have been studied by X-ray crystallography. One crystal form (crystal form II), which D-monellin greatly favors in crystallization, shows a completely different dimer contact to all L-monellin crystals reported to date.

Online July 1998


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Acta Cryst. (1998). D54, 501-509  [ doi:10.1107/S0907444997013954 ]

Structure of d(CACGCG)\cdotd(CGCGTG) in Crystals Grown in the Presence of RutheniumIII Hexammine Chloride

P. Karthe and N. Gautham

Synopsis: The structure at 1.64 Å resolution is a left-handed Z-DNA helix. It suggests a non-specific role for the metal ion in helix stabilization.

Online July 1998


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Acta Cryst. (1998). D54, 510-521  [ doi:10.1107/S0907444997013644 ]

Structure of a Basic Phospholipase A2 from Agkistrodon halys Pallas at 2.13 Å Resolution

K. Zhao, S. Song, Z. Lin and Y. Zhou

Synopsis: The structure has been determined by molecular replacement and compared with the acidic isoform.

Online July 1998


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Acta Cryst. (1998). D54, 522-546  [ doi:10.1107/S0907444997013656 ]

Refinement of Triclinic Hen Egg-White Lysozyme at Atomic Resolution

M. A. Walsh, T. R. Schneider, L. C. Sieker, Z. Dauter, V. S. Lamzin and K. S. Wilson

Synopsis: The X-ray crystal structures of the triclinic form of hen egg-white lysozyme refined against data extending to 0.92 Å at 120 K and 0.95 Å at 295 K are described. The data allowed occupancy refinement of solvent sites.

Online July 1998


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Acta Cryst. (1998). D54, 547-557  [ doi:10.1107/S0907444997013875 ]

Rfree and the Rfree Ratio. I. Derivation of Expected Values of Cross-Validation Residuals Used in Macromolecular Least-Squares Refinement

I. J. Tickle, R. A. Laskowski and D. S. Moss

Synopsis: Estimates of the expected ratio of the free R factor to the standard R factor are calculated for the cases of restrained and unrestrained refinement. Comparison of this Rfree ratio can be used to detect systematic model or weighting errors.

Online July 1998


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Acta Cryst. (1998). D54, 558-569  [ doi:10.1107/S090744499701620X ]

Structure of Holo-glyceraldehyde-3-phosphate Dehydrogenase from Palinurus versicolor Refined at 2 Å Resolution

S. Song, J. Li and Z. Lin

Synopsis: The structure of holo-glyceraldehyde-3-phosphate dehydrogenase from South China Sea lobster reveals subunit similarity and some differences from the thermophilic enzymes.

Online July 1998


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Acta Cryst. (1998). D54, 570-576  [ doi:10.1107/S0907444997013097 ]

1.76 Å Structure of a Pyrimidine Start Alternating A-RNA Hexamer r(CGUAC)dG

R. Biswas, S. N. Mitra and M. Sundaralingam

Synopsis: The crystal structure of r(CGUAC)dG with two independent duplexes in the asymmetric unit has been determined at high resolution. The 2'-hydroxyl groups are engaged in water-mediated hydrogen bonding to all three groups of the nucleotide, i.e.., base, sugar and phosphate.

Online July 1998


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Acta Cryst. (1998). D54, 577-583  [ doi:10.1107/S090744499701559X ]

Structure of the DNA Decamer d(GGCAATTGCG) Contains both Major- and Minor-Groove Binding G·(G·C) Base Triplets

C. M. Nunn and S. Neidle

Synopsis: G·(G·C) base triplets formed by 5'-G and G-3' binding with the B-DNA octamer duplex d(GCAATTGC)2 are described.

Online July 1998


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Acta Cryst. (1998). D54, 584-588  [ doi:10.1107/S090744499701500X ]

Structural Evidence for the Aromatic-(i+1) Amine Hydrogen Bond in Peptides: L-Tyr-L-Tyr-L-Leu Monohydrate

T. Steiner

Synopsis: In the crystal structure of L-Tyr-L-Tyr-L-Leu monohydrate, a short intramolecular contact is formed between a Tyr side chain and the peptide NH of the next residue. Reasons are given why this contact represents a weak hydrogen bond.

Online July 1998


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Acta Cryst. (1998). D54, 589-597  [ doi:10.1107/S0907444997015849 ]

Structure of the Kunitz-Type Soybean Trypsin Inhibitor (STI): Implication for the Interactions Between Members of the STI Family and Tissue-Plasminogen Activator

P. de Meester, P. Brick, L. F. Lloyd, D. M. Blow and S. Onesti

Synopsis: Crystals of the free soybean trypsin inhibitor have been obtained and the structure determined by molecular replacement. The structure allows a comparison to be made of the reactive-site loop in the complexed and uncomplexed forms and gives an insight into the possible interactions between the homologous Erythrina trypsin inhibitor and tissue-type plasminogen activator.

Online July 1998


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Acta Cryst. (1998). D54, 598-609  [ doi:10.1107/S0907444997016193 ]

Atomic Resolution Structure of Human HBP/CAP37/Azurocidin

S. Karlsen, L. F. Iversen, I. K. Larsen, H. J. Flodgaard and J. S. Kastrup

Synopsis: Human heparin binding protein crystals diffract to atomic resolution when flash-frozen at 120 K. The fully refined 1.1  Å structure is described.

Online July 1998


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Acta Cryst. (1998). D54, 610-614  [ doi:10.1107/S0907444997020295 ]

On the Choice of an Optimal Wavelength in Macromolecular Crystallography

A. Teplyakov, G. Oliva and I. Polikarpov

Synopsis: Experiments carried out at EMBL synchrotron beamlines at DESY show there is an advantage in using wavelengths longer than 1 Å for X-ray data collection from small frozen protein crystals.

Online July 1998


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Acta Cryst. (1998). D54, 615-621  [ doi:10.1107/S0907444997018982 ]

Direct Phase Determination in Protein Electron Crystallography: Aquaporin Channel-Forming Integral Membrane Protein

D. L. Dorset and B. K. Jap

Synopsis: The projected aquaporin structure is determined in projection to 6 Å resolution by direct methods. Helix centres are located but helix tilt is not evident in the potential maps.

Online July 1998


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Acta Cryst. (1998). D54, 622-628  [ doi:10.1107/S0907444997019008 ]

Macromolecular Crystal Annealing: Overcoming Increased Mosaicity Associated with Cryocrystallography

J. M. Harp, D. E. Timm and G. J. Bunick

Synopsis: Macromolecular crystal annealing is a simple process that can offset increased mosaicity caused by flash-cooling. The process offers many benefits, such as the recovery of mishandled crystals, and extends the application of cryocrystallography.

Online July 1998


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Acta Cryst. (1998). D54, 629-635  [ doi:10.1107/S0907444998005423 ]

Structure Determination of a 16.8 kDa Copper Protein at 2.1 Å Resolution Using Anomalous Scattering Data with Direct Methods

I. Harvey, Q. Hao, E. M. H. Duke, W. J. Ingledew and S. S. Hasnain

Synopsis: The structure of rusticyanin has been determined at 2.1 Å resolution by combining direct methods with the single wavelength anomalous scattering of copper. The results provide clear demonstration of the power of the method in solving a de novo protein structure.

Online July 1998


crystallization papers


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Acta Cryst. (1998). D54, 636-638  [ doi:10.1107/S0907444997012249 ]

Crystallization and preliminary X-ray study of saporin, a ribosome-inactivating protein from Saponaria officinalis

C. Savino, L. Federici, A. Brancaccio, R. Ippoliti, E. Lendaro and D. Tsernoglou

Synopsis: The single-chain ribosome-inactivating protein saporin isoform 6 isolated from the seeds of S. officinalis has been crystallized under high-salt conditions. The crystals belong to the tetragonal system, space group P4122 or P4322 and diffract to 2.0 Å.

Online July 1998


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Acta Cryst. (1998). D54, 639-642  [ doi:10.1107/S0907444997014121 ]

Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II

A. L. Lamb, X. Wang, J. L. Napoli and M. E. Newcomer

Synopsis: Retinal dehydrogenase type II was purified from an E. coli overexpression system and crystallized in two separate conditions. Two crystal forms were obtained. Only the crystals belonging to space group P212121, grown in conditions which minimize O2 exposure, produced high quality X-ray diffraction data.

Online July 1998


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Acta Cryst. (1998). D54, 643-646  [ doi:10.1107/S0907444997015011 ]

Crystallization of human complement component C5

R. G. Discipio, L. Jenner, S. Thirup, L. Sottrup-Jensen, J. Nyborg and E. Stura

Synopsis: With the application of synchrotron radiation, a diffraction resolution of 3.3 Å has been obtained from crystals of human complement component C5.

Online July 1998


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Acta Cryst. (1998). D54, 647-649  [ doi:10.1107/S0907444997016156 ]

Purification, crystallization and preliminary X-ray analysis of the Escherichia coli phytase

Z. Jia, S. Golovan, Q. Ye and C. W. Forsberg

Synopsis: Phytase from E. coli has been crystallized using a bulk crystallization method without, a conventional precipitant. The enzyme is a 6-phytase involved in the hydrolysis of phytic acid.

Online July 1998


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Acta Cryst. (1998). D54, 650-653  [ doi:10.1107/S0907444997018854 ]

Crystallization and preliminary X-ray crystallographic studies of the native and chemically modified anion-selective porin from Comamonas acidovorans

K. Zeth, V. Schnaible, M. Przybylski, W. Welte, K. Diederichs and H. Engelhardt

Synopsis: The pore-forming outer membrane protein (porin) Omp32 was crystallized in three different crystal forms of space group R3. Two forms were obtained with native porin, the third form occurred with Omp32 containing succinylated lysine residues.

Online July 1998


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Acta Cryst. (1998). D54, 654-656  [ doi:10.1107/S0907444997015655 ]

Crystallization and preliminary crystallographic studies of chloroplast NADP-dependent malate dehydrogenase from Flaveria bidentis

K. H. R. MacPherson, A. R. Ashton, P. D. Carr, S. J. Trevanion, D. Verger and D. L. Ollis

Synopsis: Crystals of this enzyme have been produced and X-ray data collected to 2.8 Å. The space group, unit-cell dimensions and Matthews coefficient have been determined.

Online July 1998


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Acta Cryst. (1998). D54, 657-658  [ doi:10.1107/S0907444997018994 ]

Crystallization and preliminary X-ray analysis of IND, an enzyme with indole oxygenase activity from Chromobacterium violaceum

E. Cheah, K. MacPherson, D. Quiggin, P. Keese and D. L. Ollis

Synopsis: The crystallization of a flavoprotein with indole oxygenase activity is described.

Online July 1998


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Acta Cryst. (1998). D54, 659-661  [ doi:10.1107/S0907444997016235 ]

Crystallization and preliminary X-ray diffraction analysis of aspartate aminotransferase from Saccharomyces cerevisiae

C. J. Jeffery, T. Barry, S. Doonan, G. A. Petsko and D. Ringe

Synopsis: Crystals of S. cerevisiae cytoplasmic aspartate aminotransferase that diffract to spacings of 2 Å have been obtained in the presence of pyridoxal phosphate and maleic acid.

Online July 1998


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Acta Cryst. (1998). D54, 662-664  [ doi:10.1107/S0907444997017824 ]

Crystallization and preliminary X-ray studies of allophycocyanin from red alga Porphyra yezoensis

J.-Y. Liu, J.-P. Zhang, Z.-L. Wan, D.-C. Liang, J.-P. Zhang and H.-J. Wu

Synopsis: Allophycocyanin from red alga P. yezoensis has been crystallized in three crystal forms.

Online July 1998


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Acta Cryst. (1998). D54, 665-667  [ doi:10.1107/S0907444997019859 ]

Scilla campanulata agglutinin crystallized in complex with the trimannoside \boldalpha-D-Man-(1\rightarrow6)-[[alpha]-D-Man-(1\rightarrow3)]-[alpha]-D-Man

L. M. Wright, P. J. Rizkallah, S. D. Wood and C. D. Reynolds

Synopsis: The crystallization and preliminary X-ray analysis of S. campanulata agglutinin complexed with a trisaccharide is reported. The complex crystallizes in space group C2 with six subunits per asymmetric unit and has been solved by molecular replacement at 2.5 Å resolution.

Online July 1998


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Acta Cryst. (1998). D54, 668-670  [ doi:10.1107/S0907444997016211 ]

Preliminary X-ray crystallographic study of wild-type and mutant ribulose-1,5-bisphosphate carboxylase/oxygenase from Chlamydomonas reinhardtii

A. Yen, E. J. Haas, K. M. Selbo, C. R. Ross II, R. J. Spreitzer and J. J. Stezowski

Synopsis: Wild-type and several mutant forms of ribulose-1,5-bisphosphate carboxylase/oxygenase from the green alga, C. reinhardtii, have been crystallized. It is anticipated that the solution of these related structures will reveal the subtle interactions that influence the specificity of the enzyme for CO2 and O2.

Online July 1998


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Acta Cryst. (1998). D54, 671-674  [ doi:10.1107/S0907444997018076 ]

Characterization, crystallization and preliminary X-ray investigation of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus

T. M. Fleming, C. E. Jones, P. W. Piper, D. A. Cowan, M. N. Isupov and J. A. Littlechild

Synopsis: GAPDH from S. solfataricus has been crystallized. The crystals diffract to 2.4 Å and belong to the space group P41212 or P43212 with unit-cell parameters a = b = 101.57, c = 179.81 Å.

Online July 1998


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Acta Cryst. (1998). D54, 675-677  [ doi:10.1107/S0907444997017836 ]

Crystallization and preliminary diffraction studies of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2

P. C. E. Moody, N. Shikotra, C. E. French, N. C. Bruce and N. S. Scrutton

Synopsis: Crystals of PETN reductase belong to space group P212121 and diffract beyond 1.8 Å. Molecular replacement calculations using Old Yellow enzyme as a search model give a unique solution.

Online July 1998


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Acta Cryst. (1998). D54, 678-680  [ doi:10.1107/S090744499701785X ]

Crystallization of 5-keto-4-deoxyuronate isomerase from Escherichia coli

P. Dunten, H. Jaffe and R. R. Aksamit

Synopsis: 5-Keto-4-deoxyuronate isomerase from E. coli has been crystallized from ammonium sulfate and a suitable cryoprotectant has been identified.

Online July 1998


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Acta Cryst. (1998). D54, 681-683  [ doi:10.1107/S0907444997017848 ]

Crystallization and preliminary X-ray studies of Pseudomonas putida histidine ammonium-lyase

B. Teo, R. D. Kidd, J. Mack, A. Tiwari, D. Hernandez, A. T. Phillips and G. K. Farber

Synopsis: Histidine ammonium-lyase from P. putida was expressed in E. coli, purified to homogeneity, and crystallized by the vapour-diffusion method using polyethylene glycol 3350 as the precipitant. The crystals, which diffract to at least 2.5 Å resolution, exhibit the symmetry of space group P212121, with unit-cell parameters a = 89.7, b = 138.2 and c = 164.8 Å.

Online July 1998


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Acta Cryst. (1998). D54, 684-686  [ doi:10.1107/S0907444997018970 ]

Preliminary crystallographic investigations of recombinant GDP-4-keto-6-deoxy-D-mannose epimerase/reductase from E. coli

M. Tonetti, M. Rizzi, P. Vigevani, L. Sturla, A. Bisso, A. De Flora and M. Bolognesi

Synopsis: The GDP-L-fucose producing enzyme has been crystallized in a trigonal form suitable for high-resolution studies.

Online July 1998


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Acta Cryst. (1998). D54, 687-689  [ doi:10.1107/S0907444997018866 ]

Crystallization and preliminary X-ray analysis of [beta]-glucan exohydrolase isoenzyme ExoI from barley (Hordeum vulgare)

M. Hrmova, J. N. Varghese, P. B. Høj and G. B. Fincher

Synopsis: Crystals of a barley [beta]-glucan exohydrolase diffract to at least 2.2 Å resolution. The crystals and their heavy-metal derivatives should allow the first structure of a family 3 glycosyl hydrolase to be solved.

Online July 1998


short communications


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Acta Cryst. (1998). D54, 690-692  [ doi:10.1107/S0907444997015023 ]

Subcloning, crystallization and preliminary X-ray analysis of the signal receiver domain of ETR1, an ethylene receptor from Arabidopsis thaliana

A. A. Grantz, H. J. Müller-Dieckmann and S.-H. Kim

Synopsis: Crystals of both native and a selenomethionine-substituted form of the signal receiver domain of ETR1, an ethylene receptor from A. thaliana, have been obtained and shown to diffract to 2.1 and 2.5 Å, respectively.

Online July 1998


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Acta Cryst. (1998). D54, 693-696  [ doi:10.1107/S0907444997019732 ]

Preliminary X-ray analysis of a C2-like domain from protein kinase C-[delta]

H. Pappa, L. V. Dekker, P. J. Parker and N. Q. McDonald

Synopsis: This paper reports the crystallization and characterization of a C2-like domain from PKC-[delta]. The production of selenomethionine-substituted material is described and will assist the solution of the phase problem.

Online July 1998


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Acta Cryst. (1998). D54, 697-699  [ doi:10.1107/S0907444997020222 ]

Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein from Escherichia coli

B. S. Smith, B. Kobe, R. Kurumbail, S. K. Buchanan, L. Venkatramani, D. van der Helm and J. Deisenhofer

Synopsis: Diffraction-quality crystals have been obtained of the integral membrane protein ferric enterobactin receptor from the outer membrane of E. coli using the zwitterionic detergent lauryldimethylamine oxide, the precipitants PEG 1000 and NaCl, and the additive heptane-1,2,3-triol. The crystals are in orthorhombic space group C2221 with a = 112.2, b = 137.2 and c = 135.4 Å and diffract to 2.5 Å resolution.

Online July 1998


fast communications


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Acta Cryst. (1998). D54, 700-702  [ doi:10.1107/S0907444997020040 ]

Structure of type III antifreeze protein at 277 K

Q. Ye, E. Leinala and Z. Jia

Synopsis: Type III antifreeze protein was crystallized at 277 K. The resulting structure is essentially identical to the room-temperature structure, thereby supporting the biological relevance of the latter structure.

Online July 1998


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Acta Cryst. (1998). D54, 703-706  [ doi:10.1107/S0907444997020052 ]

Protein crystals orientation in a magnetic field

J. P. Astier, S. Veesler and R. Boistelle

Synopsis: Crystallization experiments of different proteins were carried out in the presence of a magnetic field. Crystals are found oriented in the field.

Online July 1998


addenda and errata


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Acta Cryst. (1998). D54, 707  [ doi:10.1107/S0907444998006817 ]

Low-resolution structural characterization of the arginine repressor/activator from Bacillus subtilis: a combined X-ray crystallographic and electron microscopical approach. Erratum

N. M. Glykos, A. Holzenburg and S. E. V. Phillips

Synopsis: A correction to the paper by Glykos, Holzenburg & Phillips [Acta Cryst. (1998). D54, 215-225].

Online July 1998


book reviews


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Acta Cryst. (1998). D54, 708-709  [ doi:10.1107/S0907444998003011 ]

Macromolecular crystallography. Part A. Methods in Enzymology

Online July 1998


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Acta Cryst. (1998). D54, 709-710  [ doi:10.1107/S0907444998003023 ]

Macromolecular crystallography. Part B. Advances in Enzymology

Online July 1998


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