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  • Blackwell Publishing Ltd  (466)
  • Copernicus  (320)
  • International Union of Crystallography (IUCr)
  • 1
    Electronic Resource
    Electronic Resource
    Structure of copper- and oxalate-substituted human lactoferrin at 2.0 Å resolution (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 302-316 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The three-dimensional structure of human dicupric monooxalate lactoferrin, Cu2oxLf, has been determined to 2.0 Å resolution, using X-ray diffraction data collected by diffractometry to 2.5 Å resolution, and oscillation photography on a synchrotron source to 2.0 Å resolution. Difference electron-density maps calculated between Cu2oxLf and both dicupric lactoferrin, Cu2Lf, and diferric lactoferrin, Fe2Lf, showed that the oxalate had replaced a carbonate in the C-terminal binding site, and that, relative to Cu2Lf, there were no significant differences in the N-terminal site. The structure was then refined crystallographically by restrained least-squares methods. The final model, in which the r.m.s. deviation in bond distances is 0.017 Å, contains 5314 protein atoms (691 residues), two Cu2+ ions, one bicarbonate ion, one oxalate ion, 325 solvent molecules and one sugar residue. The crystallographic R factor of 0.193 is for 46 134 reflections in the range 8.0 to 2.0 Å resolution. The oxalate ion is coordinated to copper in a 1,2-bidentate fashion, and the added bulk of the anion results in the rearrangement of the side chains of nearby arginine and tyrosine residues. No other major alterations in the molecule can be observed, the overall protein structure being the same as that for Cu2Lf and Fe2Lf.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994000491
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  • 2
    Electronic Resource
    Electronic Resource
    Structure of recombinant human lactoferrin expressed in Aspergillus awamori (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 403-407 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Human lactoferrin (hLf) has considerable potential as a therapeutic agent. Overexpression of hLf in the fungus Aspergillus awamori has resulted in the availability of very large quantities of this protein. Here, the three-dimensional structure of the recombinant hLf has been determined by X-ray crystallography at a resolution of 2.2 Å. The final model, comprising 5339 protein atoms (residues 1–691, 294 solvent molecules, two Fe3+and two CO_3^{2-} ions), gives an R factor of 0.181 (free R = 0.274) after refinement against 32231 reflections in the resolution range 10–2.2 Å. Superposition of the recombinant hLf structure onto the native milk hLf structure shows a very high level of correspondence; the main-chain atoms for the entire polypeptide can be superimposed with an r.m.s. deviation of only 0.3 Å and there are no significant differences in side-chain conformations or in the iron-binding sites. Dynamic properties, as measured by B-value distributions or iron-release kinetics, also agree closely. This shows that the structure of the protein is not affected by the mode of expression, the use of strain-improvement procedures or the changes in glycosylation due to the fungal system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998011226
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  • 3
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    Electronic Resource
    Expression, crystallization and preliminary characterization of methylmalonyl coenzyme A epimerase from Propionibacterium shermanii (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 706-708 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Methylmalonyl-CoA epimerase (MMCE) is an enzyme that interconverts the R and S epimers of methylmalonyl-CoA in the pathway that links propionyl-CoA with succinyl-CoA. This is used for both biosynthetic and degradative processes, including the breakdown of odd-numbered fatty acids and some amino acids. The enzyme has been expressed in Escherichia coli both as the native enzyme and as its selenomethionine (SeMet) derivative. Crystals of both forms have been obtained by vapour diffusion using monomethylether PEG 2000 as precipitant. The native MMCE crystals are orthorhombic, with unit-cell parameters a = 56.0, b = 114.0, c = 156.0 Å, and the SeMet-MMCE crystals are monoclinic, with unit-cell parameters a = 43.6, b = 78.6, c = 89.4 Å, β = 92.0°; both diffract to better than 2.8 Å resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901002050
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  • 4
    Electronic Resource
    Electronic Resource
    Search designs for protein crystallization based on orthogonal arrays (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 429-440 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: In protein crystallography, the initial experimental problem is the identification of physical and chemical conditions that will support nucleation and crystal growth. Ideally, experiments to search for such conditions would be based on a full-factorial structure, with variation in the temperature and solution composition. However, consideration of even a moderate number of possibilities for the composition of the system will result in factorial experiments which may be prohibitively large. In this paper it is proposed that search experiments for protein crystallization might be based on orthogonal arrays. These are subsets of full-factorial experiments which possess a great deal of symmetry, such that a uniform distribution of points throughout the experimental region is preserved. Such experiments have reasonable size, explore the proposed experimental region in a systematic fashion, and form a logical basis for a sequential approach to the search for crystallization conditions. Examples of such initial search experiments are given, and their application to some recent protein crystallization problems in this laboratory is described briefly. The relationship of this approach to other protein crystallization search procedures is also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444993014374
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  • 5
    Electronic Resource
    Electronic Resource
    Enzymatic deglycosylation as a tool for crystallization of mamalian binding proteins (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 380-384 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Enzymatic deglycosylation has been used in attempts to crystallize several glycoproteins with the aim of overcoming the problems resulting from heterogeneity and flexibility of the attached glycan chains. An endoglycosidase preparation from Flavobacterium meningosepticum, comprising the enzymes endo F and PNGase-F, was used in experiments on the mammalian binding proteins lactoferrin and haemopexin. Significant differences were found in the susceptibility of different proteins to deglycosylation. For human lactoferrin (Lf) and its recombinant N-terminal half-molecule (LfN), deglycosylation was rapid and complete, and was essential for obtaining high-quality crystals of both apo-Lf and LfN; for bovine Lf, however, complete deglycosylation did not occur. Similarly, for rabbit haemopexin the carbohydrate chain on the C-terminal domain was easily removed, but the three chains on the N-terminal domain proved more resistant and their removal led to some fragmentation of the protein. Nevertheless, this approach provided the only means of crystallizing the C-terminal domain and is likely to be useful for other glycoproteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444993013435
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  • 6
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    Electronic Resource
    Crystallization and preliminary X-ray analysis of native and recombinant human bile-salt dependent lipase: strategies for improvement of diffraction quality (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 478-480 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Human bile-salt dependent lipase (BSDL), secreted into both the digestive tract and human milk, is integral to the effective absorption of dietary lipids. In attempts to obtain crystals suitable for high-resolution X-ray crystallographic studies, various forms of the enzyme have been crystallized, including native and desialidated human milk BSDL and both intact recombinant BSDL and a truncated form lacking the heavily glycosylated C-terminal repeat region. Trigonal crystals of native BSDL, with unit-cell parameters a = b = 90.0, c = 156.1 Å, were obtained using 15–20%(w/v) PEG 8000 as precipitant. These crystals diffract to 3.5 Å along the unique axis, but to only 5–7 Å in orthogonal directions. Crystals of recombinant truncated BSDL grown from 15–20%(w/v) PEG 6000 are orthorhombic, space group P212121, with unit-cell parameters a = 59.2, b = 90.0, c = 107.7 Å, and diffract to 2.6 Å resolution. These are suitable for structural analysis by X-ray crystallography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900000986
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  • 7
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    Electronic Resource
    Subunit dissociation and reassociation leads to preferential crystallization of haemoglobin Bart's (γ4) from solutions of human embryonic haemoglobin Portland (ζ2γ2) at low pH (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 921-924 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A variety of human haemoglobins (Hbs) are produced at different stages of human development, including three embryonic Hbs, foetal Hb and adult Hb. All are heterotetramers. During crystallization experiments on human embryonic Hb Portland (ζ2γ2), it was discovered by crystallographic and biochemical analysis that the homotetramer Hb Bart's (γ4) preferentially crystallizes from ζ2γ2 solutions below pH 5. This results from dissociation of Hb Portland into γ2 dimers and ζ monomers and has interesting implications for subunit interactions and tetramer stability in Hbs. It also makes possible a full crystallographic analysis of Hb Bart's, which is of considerable medical significance because of its presence in the red blood cells of millions of people worldwide who suffer from α-thalassaemia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901004516
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  • 8
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction studies of a cobalt-substituted derivative of the iron-dependent alcohol dehydrogenase from Zymomonas mobilis (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 218-220 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The iron-dependent alcohol dehydrogenase from Zymomonas mobilis has been crystallized in a form suitable for X-ray diffraction studies. The crystals grew in hanging drops by vapor diffusion, equilibrating with a solution comprising 25–27% methoxypolyethylene glycol 5000 and 1 mM Co2+ in a 0.2 M succinic acid/potassium hydroxide buffer at pH 5.5–5.7 at 281 K. Crystals are tetragonal, P4122 (or P4322), with unit-cell dimensions a = b = 125.7, c = 248.1 Å. Four molecules comprise the asymmetric unit, and a self-rotation function indicates twofold local symmetry perpendicular to the unique axis and 15° from a crystallographic twofold axis. Diffraction data to 3.0 Å have been collected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995009103
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  • 9
    Electronic Resource
    Electronic Resource
    Effects of temperature and current discharge on the concentration and photosynthetic activity of the phytoplankton in the upper Mississippi River (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Freshwater biology 9 (1979), S. 0 
    Details
    ISSN: 1365-2427
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: SUMMARY. Temperature and current discharge regulated phytoplanktonic concentration, chlorophyll-a concentration, the light-saturated rate of photosynthesis (Pmax), and photosynthetic capacity (Pcap) in the Mississippi River at Prairie Island, Minnesota. The chlorophyll-a maximum was 48 mg m−3 in 1975, a wet year with a high current discharge, and 190 mg m−3 in 1976, a relatively dry year. The highest values of Pmax were 0.37 (mgO2 I−1h−1) in 1975 and 1.60 in 1976. Pcap varied from 3 to 21 (gO2 per g chlorophyll-a h−1) both years, and its value was highly correlated with temperature. The temperature optimum shifted from 16°C for Pcap in the spring, to greater than 28°C in the summer. Multiple regression analysis indicated a second-order relationship of Pcap in the spring to temperature. Other independent variables explained only negligible variation of Pcap.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2427.1979.tb01502.x
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  • 10
    Electronic Resource
    Electronic Resource
    Fine-layer depth relationships of lakewater chemistry, planktonic algae and photosynthetic bacteria in meromictic Lake Fidler, Tasmania (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Freshwater biology 15 (1985), S. 0 
    Details
    ISSN: 1365-2427
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: SUMMARY. 〈list xml:id="l1" style="custom"〉1Use of a multi-column thin-layer pneumatic sampler and modified analytic procedures has enabled resolutions of chemical and biological strata at 2.5 or 5.0 cm depth intervals. Examination of meromictic Lake Fidler, Tasmania, indicates the presence of a thin, intense stratum of bacteriochlorohyll d in the upper monimolimnion, associated with a discrete stratum of Chlorobium cf. limicola at the microaerobic interface between the oxygenated and sulphide-rich zones.2Algae included small populations of Chlorophyceae, Chrysophyceae, Bacillariophyceae and Cryptophyceae. Bacteria included microaerophils and obligate anaerobes, pigmented and colourless, in well-defined strata in the upper monimolimnion. A population of the microcrustacean Calamoecia tasmanica tasmanica was present in the mixolimnion. Chaoborus larvae were concentrated within the Chlorobium layer.3The chemical profile of Lake Fidler was stable, with a chemocline constant in position relative to the lake bottom. The surface water levels rose and fell through a distance of 1m in conjunction with heavy rainfall in the rainforest, and with river level variation, but had no measurable effect on the absolute position of the chemocline. Marked heterogeneity of dissolved substances at depths in the vicinity of bacteria suggested endogenous influence on pH and gelbstoff (‘gilvin’ in Australia).4Downwelling light attenuation was influenced primarily by gelbstoff (‘gilvin’) in the mixolimnion, with only red light (peak at 700 nm) measurable below 2 m. Light was absorbed mainly by Chlorobium in the monimolimnion, and was unmeasurable deeper than 3 m.5The absorption spectrum of the bacteriochlorophyll d in vivo, with a maximum absorbance at 721 nm, corresponds with the available downwelling light penetrating the mixolimnion to the Chlorobium layer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2427.1985.tb00245.x
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