Axial ranking of residues in collagen in relation to edge association and fibril formation

In our earlier analysis of intermolecular interactions between collagen molecules, a major concern with the program employed is that it compared numbers of interactions between residues located on edges of defined, identical width and thus would not necessarily compare the same number of residues in each edge. This would be particularly true of some values of θ where well-defined vertical ranking of residues occurs. We have examined ranking of residues in relation to intermolecular edge association between bovine skin [α1(I)]₃ model collagen molecules by utilizing two different methods of counting intermolecular interactions between residues. The interaction peaks at θ = 27.69° and 36.00° are absent or relatively less intense in the plots obtained by utilizing radial distances between interacting residues instead of vertical bands of defined width. These studies suggest caution in accepting recently reported analyses of superhelix coiling of the collagen molecule which point to values of 27.69° or 36.00° for the twist of the superhelix. Although intramolecular interactions clearly point to interaction of collagen molecules at D intervals, they are insufficiently restricted in distribution to provide a reliable estimate of the superhelix angle by procedures so far employed.     

Two-dimensional motion of DNA bands during pulsed-field gel electrophoresis. II. Effect of field angle

In pulsed-field gel electrophoresis, megabase DNAs are well separated if the angle θ between the two electric fields is 120° but not if θ = 90°. To elucidate the molecular basis for this observation, we measured the instantaneous position (x, y) and velocity (v_x, v_y) of a band of G-DNA (670 kb) while the field switched direction, for 90° ≤ θ ≤ 102°. For θ = 120° and long pulse period T. The band retraced the last segment of the preceding pulse before moving in- the new field direction. The retracing wax done at a velocity much greater than the average forward velocity. For θ = 90°, rather than retrace itself, the path during one pulse appeared to originate from a point beyond that reached in the previous pulse, end the velocity showed only a brief backward spike. A Monte Carlo simulation that included tube-length fluctuations and hernias was carried out for a model DNA chain moving through a three-dimensional network of interconnected pores, with parameters corresponding to the DNA size, agarose concentration, and field strength of the experiments, Both the xy path and the instantaneous velocities of the simulation were in excellent agreement with experiment for 90° ≤ θ ≤ 120°. When the field changed direction in the simulation, hernias often advanced from both ends in the new field direction. In the 120° case, those near the erstwhile trailing segments of the chain soon established superiority because chain tension and a component of the new field aided their growth. For θ = 90° and long T, however, segments from the head end were more likely to continue to lead because there was often an excess of relaxed segments there, and no component of the field aided either end. © 1995 John Wiley & Sons, Inc.     

Dielectric relaxation of collagen in aqueous solutions

The complex dielectric constant of collagen in aqueous solutions (polymer concentration, C_p = 0.02–0.2%) was measured at 10°C in the frequency range from 3 Hz to 30 kHz. The loss peak for C_p = 0.02% is located at 90 Hz and the dielectric relaxation time τ_D is estimated to be 1.8 ± 0.3 msec. The τ_D agrees well with the rotational relaxation time estimated from the reduced viscosity, and the relaxation is ascribed to the end-over-end rotation of the molecule. The C_p dependence of τ_D and the dielectric increment Δε are interpreted in terms of the aggregation of molecules. The dipole moment of a molecule, obtained from Δε at C_p = 0.02% and pH 6.5, is (5.2 ± 0.2) × 10⁴D, which is explained by the asymmetrical distribution of the ionized side chains of the molecule.     

The effect of deuterium oxide on the stability of the collagen model peptides H‐(Pro‐Pro‐Gly)10‐OH,H‐(Gly‐Pro‐4(R)Hyp)9‐OH,and Type I collagen

The collagen triple helix has a larger accessible surface area per molecular mass than globular proteins, and therefore potentially more water interaction sites. The effect of deuterium oxide on the stability of collagen model peptides and Type I collagen molecules was analyzed by circular dichroism and differential scanning calorimetry. The transition temperatures (T_m) of the protonated peptide (Pro‐Pro‐Gly)₁₀ were 25.4 and 28.7°C in H₂O and D₂O, respectively. The increase of the T_m of (Pro‐Pro‐Gly)₁₀ measured calorimetrically at 1.0°C min^?1 in a low pH solution from the protonated to the deuterated solvent was 5.1°C. The increases of the T_m for (Gly‐Pro‐4(R)Hyp)₉ and pepsin‐extracted Type I collagen were measured as 4.2 and 2.2°C, respectively. These results indicated that the increase in the T_m in the presence of D₂O is comparable to that of globular proteins, and much less than reported previously for collagen model peptides [Gough and Bhatnagar, J Biomol Struct Dyn 1999, 17, 481–491]. These experimental results suggest that the interaction of water molecules with collagen is similar to the interaction of water with globular proteins, when the ratio of collagen to water is very small and collagen is monomerically dispersed in the solvent. © 2009 Wiley Periodicals, Inc. Biopolymers 93: 93–101, 2010. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com     

The crystal structure of 2-deoxy-β-d-arabino-hexopyranose at −150°

2-Deoxy-β-d-arabino-hexopyranose, C₆H₁₂O₅, is orthorhombic, P2₁2₁2₁, with cell dimensions at ?150° [20°], a = 6.484(2) [6.510(3)], b = 10.364(2) [10.427(4)], c = 11.134(3) [11.153(5)] Å, V = 748.2 [757.1] ų, Z = 4, D_x = 1.457 [1.440], and D_m = [1.455] g.cm^?3. The intensities of 1269 reflections were measured by using MoKα radiation. The structure was solved by direct methods, and refined by full-matrix least-squares, with anisotropic, thermal parameters for the carbon and oxygen atoms, and isotropic parameters for the hydrogen atoms. The pyranose has the ⁴C₁(d) conformation, with puckering parameters Q = 0.563 Å, θ = 3.9°, and ? = 350.3°. The departure from ideality is very small, and less than that in β-d-glucopyranose, Q = 0.584 Å and θ = 6.9°. The β-glycosidic, CO bond is short, 1.383(4) Å, and the OCOH torsion angle is ?87°, consistent with the anomeric effect. The hydrogen-bonding scheme consists of infinite chains, with side chains terminating at a ring-oxygen atom.     

Thermal properties of collagen in helical and random coiled states in the temperature range from 4° to 300°K

The low-temperature heat capacity of collagen (in the hydrated and dehydrated states) and the large entropy of collagen in the coiled state relative to the same protein in the helical state were investigated. The heat capacity for collagen in the solid state in the temperature range 4°–50° K changes proportionally to the square of temperature (C_p ～ T²). Above 50°K there is a linear dependence (C_p ～ T). The differences in the character of temperature dependence of heat capacity for the hydrated and dehydrated collagen show the importance of the specific interaction of water molecules with polypeptide chains of this protein. The peculiarities of the temperature dependence of the heat capacity difference (ΔC_p) of hydrated denatured (random coiled) and hydrated native (helical) collagen are observed at 15°, 120°, and 240°K. These differences are caused by the varying degree of ordering of the hydrate water molecules in native and denatured collagen macromolecules. At all temperatures (4°–300°K) the entropy of the random coiled state is higher than that of collagen in the native state and at 298°K ΔS = ∫ (ΔC_p/T)dT = 0.8 cal/100 g °K.     

Acute Changes In Knee‐Extensors Torque,Fiber Pennation,and Tendon Characteristics

The aim of the current study was to examine the relationships between quadriceps torque, vastus lateralis pennation angle (θ), and patella tendon stiffness (K) at 07:45 and 17:45 h. Using short‐duration static contractions, simultaneous recordings were made of vastus lateralis (VL) electromyograph (EMG), θ and patella tendon K. Peak isometric extension torque (Peak torque Ext_corr) increased by 29.4±6.5% at a knee angle of 70° (p=0.03) in the evening compared to the morning. In the contracted muscle, a 35.0±11.0% (p=0.02) time‐of‐day (TOD)‐related change in θ (to a greater evening compared to morning θ) was observed. Morning and evening measures of θ were also made, both at rest and at a standardized force level (250 N), to separate architecture change effects from increased torque capacity effects. Significant increments in θ in both the resting muscle (13.0±5.1%, p=0.046) and during the standardized exertions (8.0±3.1%, p=0.04) were observed in the evening versus the morning. Increases in θ with TOD were significantly correlated with the 40% (p=0.018) decrease in K both during the standardized contractions (r=0.788, p<0.001) and at rest (r=0.77, p=0.026). These data show that TOD affects K and θ and that these two important factors involved in in‐vivo muscle torque generation capacity are associated. The data also show that despite the potentially deleterious effects of the direction of the changes in both K and θ with TOD, peak torque Ext_corr still shows a significant upward shift in the evening relative to the morning.     

The spatial distribution of vegetation types in the Serengeti ecosystem: the influence of rainfall and topographic relief on vegetation patch characteristics

Aim The aim of this study is to introduce a structural vegetation map of the Serengeti ecosystem and, based on the map, to test the relative influences of landscape factors on the spatial heterogeneity of vegetation in the ecosystem. Location This study was conducted in the Serengeti–Maasai Mara ecosystem in northern Tanzania and southern Kenya, between 34° and 36° E longitude, and 1° and 2° S latitude. Methods The vegetation map was produced from satellite imagery using data from over 800 ground‐truthing points. Spatial characteristics of the vegetation were analysed in the resulting map using the fragstats software package. Average patch area and nearest neighbour distance (NND) were determined for grassland, shrubland and woodland vegetation types. The heterogeneity of vegetation types was estimated with Simpson’s diversity index (D). Structural equation modelling (SEM) was used to explore the relationships between the spatial characteristics of vegetation and three predictor variables: annual rainfall, coefficient of variation (CV) in annual rainfall, and topographic moisture index (TMI). Results A vegetation map is presented along with a detailed summary of the distribution of land‐cover classes and spatial heterogeneity in the ecosystem. Significant relationships were found between vegetation diversity (D) and TMI, and also between D and average rainfall. The average area of grassland patches showed significant relationships with average rainfall, with rainfall CV and with TMI. Grassland NND was positively associated with average rainfall. Woodland patch area showed a unimodal response to average rainfall and a negative linear association with TMI. Woodland NND showed a U‐shaped association with annual rainfall and a weaker positive linear association with TMI. An acceptable model that explained variation in shrubland patch characteristics could not be identified. Main conclusions The vegetation map and analysis thereof resulted in three significant causal explanatory models that demonstrate that both rainfall and topography are important contributors to the distribution of woodlands and grasslands in the Serengeti. These findings further indicate that changes in patch characteristics have a complex interaction with rainfall and with topography. Our results are concordant with recent studies suggesting that percent woody cover in African savannas receiving less than c. 650 mm year^?1 is bounded by average annual rainfall.     

The influence of single-strand breaks on the kinetics of denaturation of DNA

The influence of single-strand breaks on the kinetics of the relaxation of DNA in a solution of low ionic strength has been investigated by a temperature jump method. The relaxation of DNA after a jump of 0.7 °C in the melting region has been monitored by measuring the extinction at 260 nm. For essentially monodisperse T4 DNA (M = 130 × 10⁶) two distinct relaxation times have been observed, that depend markedly on the initial extent of denaturation 1 ? θ. The larger relaxation time decreases from 450 sec to about 300 sec, the smaller one from 55 see to 30 when 1 ? θ increases from 0.03 to about 0.8. The dependence of these relaxation times on the average number of single-strand breaks per molecule (p) appears to be very small up to p = 100. However, the relative contribution of the slow process decreases sharply when p increases from 0.6 to 30 and remains nearly constant for larger p. The observations are discussed in the light recent theories of the kinetics of denaturation.     

An electrostatic model for collagen fibrils. The interaction of reconstituted collagen with Ca++, Na+, and Cl−

A model for the electrostatic properties of hydrated collagen fibrils, based on the concept of a “penetrable” protein, has been evaluated through studies of collagen fibrils that had been chemically modified to change their electrostatic properties,. A value of 0.28 ± 0.07 ml/g was found for the intrafibrillar space sterically inaccessible to a molecule that had an equivalent spherical radius of 4.5 Å. The net intrinsic charge on reconstituted collagen is +14 mol/mol under physiological conditions, but decreases, at constant pH, with ionic strength. A value of 7.1 for the pK of the histidine and α-amino groups in reconstituted collagen was obtained through the application of the electrostatic model to this effect. The values obtained for calcium binding parameters for collagen fibrils, under solution conditions in which the nonspecific electrostatic properties of collagen fibrils were eliminated (3–5 M tetramethyl ammonium chloride), were in agreement with values obtained in 0.16 M NaCl solutions calculated through the use of the electrostatic theory. These are 0.73 ± 0.23 and 56.2 ± 12.3 sites per molecule with intrinsic association constants of 1101 ± 386 and 21.4 ± 5.2 M^?1, respectively. The model also predicts that an average 4-mV potential difference exists between the reconstituted collagen fibrils and physiological solutions, and that collagen fibrils under such conditions have piezoelectriclike properties. The pattern of interaction of ions with collagen fibrils is such that an allosteric mechanism for the catalytic step in the mineralization of collagen is a possibility.     

Translational and rotational diffusion of tobacco mosaic virus from polarized and depolarized light scattering

The translational and rotational dynamics of tobacco mosaic virus in sodium phosphate buffer (pH =7.5) solutions has been investigated by polarized and depolarized light scattering Rayleigh linewidth studies. For concentrations ranging from 1.75 × 10^?4 g ml^?1 to 0.25 × 10^?4 g ml^?1 the translational diffusion coefficient (D_T) has been found to be slightly concentration dependent and extrapolation to zero concentration gives D₀^20°C = 0.34 ± 0.01 × 10^?7 cm²S^?1. A full analysis of the polarized spectra obtained at high and low scattering angles and the depolarized spectra at near zero scattering angles has enabled these techniques to be compared and the rotational diffusion constant D_R to be determined. At a solution concentration of 1.75 × 10^?4 g ml^?1 a mean value is found to be D_R^20°C = 350 ± 30s^?1. These values of D_T and D_R are in approximate agreement with calculations based on models of the tobacco mosaic virus molecule as a cylindrical rod.     

Helix-Forming tendencies of amino acids depend on their sequence contexts: Tripeptides AFG and FAG show incipient β-bulge formation in their crystal structures

Many of the theoretical methods used for predicting the occurrence of α-helices in peptides are based on the helical preferences of amino acid monomer residues. In order to check whether the helix-forming tendencies are based on helical preferences of monomers only or also on their sequence contexts, we synthesized permuted sequences of the tripeptides GAP, GAV, and GAL that formed crystalline helices with near α-helical conformation. The tripeptides AFG and FAG formed good crystals. The x-ray crystallographic studies of AFG and FAG showed that though they contain the same amino acids as GAF but in different sequences, they do not assume a helical conformation in the solid state. On the other hand, AFG and FAG, which contain the same amino acids but in a different sequence, exhibit nearly the same backbone torsion angles corresponding to an incipient formation of a β-bulge, and exhibit nearly identical unit cells and crystal structures. Based on these results, it appears that the helix-forming tendencies of amino acids depend on the sequence context in which it occurs in a polypeptide. The synthetic peptides AFG (L -Ala-L -Phe-Gly) and FAG (L -Phe-L -Ala-Gly), C₁₄H₁₉N₃O₄, crystallize in the orthorhombic space group P2₁2₁2₁, with a = 5. 232(1), b = 14. 622(2), c = 19. 157(3) Å, D_x = 1.329 g cm^?3, Z = 4, R = 0.041 for 549 reflections for AFG, and with a = 5. 488(2), b = 14.189 (1), c = 18.562(1) Å, D_x = 1.348 g cm^?3, Z = 4, R = 0.038 for 919 reflections for FAG. Unlike the other tripeptides GAF, GGV, GAL, and GAI, the crystals of AFG and FAG do not contain water molecule, and the molecules of AFG or FAG do not show the helical conformation. The torsion angles at the backbone of the peptide are ψ₁ = 144. 5(5)°; ?₂, ψ₂ = ?98.1(6)°, ?65.2(6)° ?₃, ψ₁₃, ψ₃₁ = 154.1(6)°, ?173.6(6)°, 6.9(8)° for AFG; and ψ₁ = 162.6(3)°; ?₂, ψ₂ = ?96.7(4)°, ?46.3(4)°; ?₃, ψ₁₃, ψ₃₁ = 150.1(3)°, ?168.7(3)°, 12.2(5)° for FAG. The conformation angles (? ψ) for residues 2 and 3 for both AFG and FAG show incipient formation of an β-bulge. © 1993 John Wiley & Sons, Inc.     

The predominant roles of the sequence periodicity in the self‐assembly of collagen‐mimetic mini‐fibrils

Collagen fibrils represent a unique case of protein folding and self‐association. We have recently successfully developed triple‐helical peptides that can further self‐assemble into collagen‐mimetic mini‐fibrils. The 35 nm axially repeating structure of the mini‐fibrils, which is designated the d‐period, is highly reminiscent of the well‐known 67 nm D‐period of native collagens when examined using TEM and atomic force spectroscopy. We postulate that it is the pseudo‐identical repeating sequence units in the primary structure of the designed peptides that give rise to the d‐period of the quaternary structure of the mini‐fibrils. In this work, we characterize the self‐assembly of two additional designed peptides: peptide Col877 and peptide Col108rr. The triple‐helix domain of Col877 consists of three pseudo‐identical amino acid sequence units arranged in tandem, whereas that of Col108rr consists of three sequence units identical in amino acid composition but different in sequence. Both peptides form stable collagen triple helices, but only triple helices Col877 self‐associate laterally under fibril forming conditions to form mini‐fibrils having the predicted d‐period. The Co108rr triple helices, however, only form nonspecific aggregates having no identifiable structural features. These results further accentuate the critical involvement of the repeating sequence units in the self‐assembly of collagen mini‐fibrils; the actual amino acid sequence of each unit has only secondary effects. Collagen is essential for tissue development and function. This novel approach to creating collagen‐mimetic fibrils can potentially impact fundamental research and have a wide range of biomedical and industrial applications.     

Dynamic light scattering from collagen solutions. I. Translational diffusion coefficient and aggregation effects

Solutions of native collagen extracted from rat tail tendons in neutral salt solution have been studied by dynamic light scattering. The spectra obtained are consistent with the presence in solution of both single rod-shaped collagen molecules and aggregates of molecules. No contribution to the spectrum has been detected at any scattering angle from rotational diffusion of single molecules, although a measurable broadening effect is expected at high angles. The translational diffusion coefficient D of single molecules, calculated from the broader spectral component, shows an anomalous dependence on collagen concentration with a maximum value of D_20,w = 8.6 ± 0.2 × 10^?12 m²/sec near the concentration 0.04% by weight. Above 0.05% D falls linearly with increasing concentration and takes the value D _20,w = 8.1 ± 0.2 × 10^?12 m²/sec at 0.064% collagen.     

Genotype‐by‐genotype specificity remains robust to average temperature variation in an aphid/endosymbiont/parasitoid system

Genotype‐by‐genotype interactions demonstrate the existence of variation upon which selection acts in host–parasite systems at respective resistance and infection loci. These interactions can potentially be modified by environmental factors, which would entail that different genotypes are selected under different environmental conditions. In the current study, we checked for a G × G × E interaction in the context of average temperature and the genotypes of asexual lines of the endoparasitoid wasp Lysiphlebus fabarum and isolates of Hamiltonella defensa, a protective secondary endosymbiont of the wasp's host, the black bean aphid Aphis fabae. We exposed genetically identical aphids harbouring different isolates of H. defensa to three asexual lines of the parasitoid and measured parasitism success under three different temperatures (15, 22 and 29 °C). Although there was clear evidence for increased susceptibility to parasitoids at the highest average temperature and a strong G × G interaction between the host's symbionts and the parasitoids, no modifying effect of temperature, that is, no significant G × G × E interaction, was detected. This robustness of the observed specificity suggests that the relative fitness of different parasitoid genotypes on hosts protected by particular symbionts remains uncomplicated by spatial or temporal variation in temperature, which should facilitate biological control strategies.     

Isolation and Characterization of Thermotolerant Gluconobacter Strains Catalyzing Oxidative Fermentation at Higher Temperatures

Thermotolerant acetic acid bacteria belonging to the genus Gluconobacter were isolated from various kinds of fruits and flowers from Thailand and Japan. The screening strategy was built up to exclude Acetobacter strains by adding gluconic acid to a culture medium in the presence of 1% D-sorbitol or 1% D-mannitol. Eight strains of thermotolerant Gluconobacter were isolated and screened for D-fructose and L-sorbose production. They grew at wide range of temperatures from 10°C to 37°C and had average optimum growth temperature between 30-33°C. All strains were able to produce L-sorbose and D-fructose at higher temperatures such as 37°C. The 16S rRNA sequences analysis showed that the isolated strains were almost identical to G. frateurii with scores of 99.36-99.79%. Among these eight strains, especially strains CHM16 and CHM54 had high oxidase activity for D-mannitol and D-sorbitol, converting it to D-fructose and L-sorbose at 37°C, respectively. Sugar alcohols oxidation proceeded without a lag time, but Gluconobacter frateurii IFO 3264^T was unable to do such fermentation at 37°C. Fermentation efficiency and fermentation rate of the strains CHM16 and CHM54 were quite high and they rapidly oxidized D-mannitol and D-sorbitol to D-fructose and L-sorbose at almost 100% within 24 h at 30°C. Even oxidative fermentation of D-fructose done at 37°C, the strain CHM16 still accumulated D-fructose at 80% within 24 h. The efficiency of L-sorbose fermentation by the strain CHM54 at 37°C was superior to that observed at 30°C. Thus, the eight strains were finally classified as thermotolerant members of G. frateurii.     

Patch edges and insect populations

Responses of insect populations may be related to patch size and patch edge responses, but it is not clear how to identify these rapidly. We used a random-walk model to identify three qualitative responses to edges: no edge effect (the null model), reflecting edges and absorbing edges. Interestingly, no edge effect meant that abundance was lower at edges than in the center of patches, and reflecting edges have similar abundance at edges and centers. We then characterized several insect species’ response within maize plots to patch edges and patch size, using a simple, quick, qualitative experiment. Coleomegilla maculata and Trichogramma spp. were the only organisms that responded to patch size and edges as patch theory and the null edge model would predict. Ostrinia nubilalis larvae and possibly Rhopalosiphum maidis and eggs of Chrysopa spp. responded to patch size and edges as predicted by an attracting edge model. Estimation of predation rates suggested that the spatial distribution of these species might be determined by predators. Edge effects or the lack thereof relative to patch size may be rapidly determined for arthropod species, which could lead to understanding the mechanism(s) underlying these effects. This information may be useful in reaction diffusion models through a scaling-up approach to predict population structure of species among patches in a landscape. Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users.     

Analysis of periodic patterns in amino acid sequences: Collagen

Methods are given for analyzing regularly spaced patterns of amino acids in proteins and applied to the α₁ chain of collagen. Fourier methods use the transform of the sequence either embedded in a very long array or folded onto a fundamental base period. Filtering through a moveable “window” of definite width is used to display almost regular features at any chosen frequency. A pattern detection method is described for patterns of general shape. Collagen has statistically significant periodicities at fractions of the stagger distance D = 670 Å. Hydrophobic groups show strong orders of 5, 6, 11; proline 5; charged groups 6, 18, 21. Charged residues mostly occur as neutral pairs. Their distribution has strong 6th and 21st orders which also appear in the changes which are paired at multiples of D. Charge pairs separated by (D + 3) residues show a strong 5D/89 pattern and may form a system of salt bridges across the fibril. There is no sign of any regular pattern of amino acids over the triple helix with a period close to its natural pitch of 30 residues. Supercoiled models with six relative turns of the contact edge between paired triple-helical strands are examined.     

The crystal and molecular structure of tetrakis(biuret)strontium(II) perchlorate

Crystals of tetrakis(biuret)strontium(II) perchlorate, [Sr((NH₂CO)₂NH)₄](ClO₄)₂, are monoclinic with a = 11.21(1), b = 7.30(1), c = 14.52(1) A, β = 98.2(2)°, D_obs = 1.976, D_calcd(Z = 2) = 1.973 g/cm³, space group P2/c. 1526 independent reflections recorded photographically by the equi-inclination. Weissenberg technique using CuKα, the intensities of which were estimated visually, were used in the structure determination. The structure was solved by Patterson and Fourier methods and refined anisotropically by diagonal least squares to an R factor of 0.094. The strontium atoms are located at special positions related by inversion. The perchlorate moieties are ionic although extensive hydrogen bonding exists between them and the primary and secondary amines of biuret. The two biuret ligands in the asymmetric unit are bonded to strontium as bidentates via the carbonyl oxygens with a small twist (10.9, 12.0°) about the oxygen-oxygen line. The six membered rings formed by the chelate ligands with strontium are folded (49.6, 1.8°) about the oxygen-oxygen line. This is attributed to packing considerations. The co-ordination polyhedron is best described as approximately D₂-222 distorted square antiprism with the bidentate ligands spanning opposite edges of the rectangular faces. To our knowledge this complex presents the first case of an eight co-ordinate non-transition metal complex, characterized by x-rays, where all of the ligands are non-ionic chemically identical oxygen donor bidentates.