Geofysiska data från Lockne-strukturen, Jämtland, Sverige

Resistivity data The resistivity data were collected with an ABEM Terrameter LS-CVES instrument along eleven profiles of variable length from 400 m to 1600 m. The distance between the electrodes was 5 m and a roll along strategy was adapted for longer profiles than 400 m. To correct for the effect of topography each profile was levelled by using a Sokkisha C3E. Profiles close to a benchmark altitude point from the Geodetic Survey of Sweden get correct absolute values, but for most of the profiles a perfect tie to a benchmark point was not possible. In these cases, the Lidar-height model was used. However, the relative height differences along all profiles are correct with centimetre precision. The resistivity measurements were performed during the summers 2013 to 2016 by Erik Sturkell, Jens Ormö, Eric Hegardt, Gabrielle Stockmann, Erik Meland, Åsa Frisk and Pierre Etienne Martin. Data processing was made with the software Res2Dinv version 3.5 from Geotomo Software and the result is presented in a pseudo section. Data for the Res2Dinv processing, the number of iterations runed and what the absolute error are given in supplementary information table S02 (which is also included in the repository). After the processed resistivity data were corrected for the topography, the results are presented in pseudo profiles along with interpretations shown in Figure 5a-c (main article), and additional data are available in the Supplementary information (which is also included in the repository). The processed resistivity data were sorted into ranges and connected to respective lithology. To present a calculation and inversion of electrical measurements as function of position (x, y, z) and electrode separation, the apparent resistivity is presented in a so called pseudo section.Motståndsmätningar Motståndsdata insamlades med ABEM Terrameter LS-CVES längs profiler av varierande längder, 400 m till 1600 m. Avståndet mellan elektroderna var 5 m och en "roll along"-metod tillämpades för profiler längre än 400 m. Precisionsavvägning genomfördes längs profilerna för att kunna genomföra en topografisk korrektion. För avvägningen användes avvägningsinstrumentet Sokkisha C3E

Differences in Backbone Dynamics of Two Homologous Bacterial Albumin-binding Modules: Implications for Binding Specificity and Bacterial Adaptation.

Proteins G and PAB are bacterial albumin-binding proteins expressed at the surface of group C and G streptococci and Peptostreptococcus magnus, respectively. Repeated albumin-binding domains, known as GA modules, are found in both proteins. The third GA module of protein G from the group G streptococcal strain G148 (G148-GA3) and the second GA module of protein PAB from P.magnus strain ALB8 (ALB8-GA) exhibit 59% sequence identity and both fold to form three-helix bundle structures that are very stable against thermal denaturation. ALB8-GA binds human serum albumin with higher affinity than G148-GA3, but G148-GA3 shows substantially broader albumin-binding specificity than ALB8-GA. The (15)N nuclear magnetic resonance spin relaxation measurements reported here, show that the two GA modules exhibit mobility on the picosecond-nanosecond time scale in directly corresponding regions (loops and termini). Most residues in G148-GA3 were seen to be involved in conformational exchange processes on the microsecond-millisecond time scale, whereas for ALB8-GA such motions were only identified for the beginning of helix 2 and its preceding loop. Furthermore, and more importantly, hydrogen-deuterium exchange and saturation transfer experiments reveal large differences between the two GA modules with respect to motions on the second-hour time scale. The high degree of similarity between the two GA modules with respect to sequence, structure and stability, and the observed differences in dynamics, binding affinity and binding specificity to different albumins, suggest a distinct correlation between dynamics, binding affinity and binding specificity. Finally, it is noteworthy in this context that the module G148-GA3, which has broad albumin-binding specificity, is expressed by group C and G streptococci known to infect all mammalian species, whereas P.magnus with the ALB8-GA module has been isolated only from humans

Structure, specificity, and mode of interaction for bacterial albumin-binding modules.

We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics