scholarly journals Unusual ultrastructure of complement-component-C4b-binding protein of human complement by synchrotron X-ray scattering and hydrodynamic analysis

1986 ◽  
Vol 233 (3) ◽  
pp. 799-807 ◽  
Author(s):  
S J Perkins ◽  
L P Chung ◽  
K B M Reid
Keyword(s):  
Electron Microscopy ◽  
Binding Protein ◽  
Complement Component ◽  
Human Complement ◽  
Hydrodynamic Analysis ◽  
X Ray ◽  
X Ray Scattering ◽  
Primary Amino ◽  
Human Complement Component ◽  
Ray Scattering

Solution X-ray-scattering experiments with the use of synchrotron radiation on the human complement-component-C4b-binding protein showed that its RG is 13 nm and that its Mr is 550,000. From the known primary amino acid sequence and estimated carbohydrate content, C4b-binding protein is inferred to have a total of 7.4 +/- 1 subunits. Heptameric computer models for C4b-binding protein were based on the X-ray-scattering curve to a resolution of 6.4 nm, and literature values for sedimentation coefficients and electron-microscopy images. The macromolecule was represented by a bundle of seven arms held together at the C-terminal end and spaced out by a base containing 23% of C4b-binding protein by volume. If the overall length of each arm is assumed to be 33 nm as seen in electron microscopy, the solution data indicate an average arm-axis angle of 5-10 degrees. The seven arms of C4b-binding protein are found to be close together, in distinction to the splayed-out images seen in electron micrographs.

Microtubule nucleation sequence studied by time-resolved x-ray scattering and electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 766-767
Author(s):  
Eva-Maria Mandelkow ◽  
Eckhard Mandelkow ◽  
Joan Bordas
Keyword(s):  
Electron Microscopy ◽  
Dynamic Equilibrium ◽  
Time Resolved ◽  
X Ray ◽  
Additional Information ◽  
X Ray Scattering ◽  
Low Concentrations ◽  
Microtubule Growth ◽  
Ray Patterns ◽  
Ray Scattering

When a solution of microtubule protein is changed from non-polymerising to polymerising conditions (e.g. by temperature jump or mixing with GTP) there is a series of structural transitions preceding microtubule growth. These have been detected by time-resolved X-ray scattering using synchrotron radiation, and they may be classified into pre-nucleation and nucleation events. X-ray patterns are good indicators for the average behavior of the particles in solution, but they are difficult to interpret unless additional information on their structure is available. We therefore studied the assembly process by electron microscopy under conditions approaching those of the X-ray experiment. There are two difficulties in the EM approach: One is that the particles important for assembly are usually small and not very regular and therefore tend to be overlooked. Secondly EM specimens require low concentrations which favor disassembly of the particles one wants to observe since there is a dynamic equilibrium between polymers and subunits.

Time-Resolved Cryo-Electron Microscopy of Oscillating Microtubules

1990 ◽  
Vol 48 (1) ◽  
pp. 502-503
Author(s):  
Eva-Maria Mandelkow ◽  
Ron Milligan
Keyword(s):  
Electron Microscopy ◽  
Dynamic Instability ◽  
Entire Solution ◽  
Reaction Scheme ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
A Chain ◽  
Ray Scattering

Microtubules form part of the cytoskeleton of eukaryotic cells. They are hollow libers of about 25 nm diameter made up of 13 protofilaments, each of which consists of a chain of heterodimers of α-and β-tubulin. Microtubules can be assembled in vitro at 37°C in the presence of GTP which is hydrolyzed during the reaction, and they are disassembled at 4°C. In contrast to most other polymers microtubules show the behavior of “dynamic instability”, i.e. they can switch between phases of growth and phases of shrinkage, even at an overall steady state [1]. In certain conditions an entire solution can be synchronized, leading to autonomous oscillations in the degree of assembly which can be observed by X-ray scattering (Fig. 1), light scattering, or electron microscopy [2-5]. In addition such solutions are capable of generating spontaneous spatial patterns [6].In an earlier study we have analyzed the structure of microtubules and their cold-induced disassembly by cryo-EM [7]. One result was that disassembly takes place by loss of protofilament fragments (tubulin oligomers) which fray apart at the microtubule ends. We also looked at microtubule oscillations by time-resolved X-ray scattering and proposed a reaction scheme [4] which involves a cyclic interconversion of tubulin, microtubules, and oligomers (Fig. 2). The present study was undertaken to answer two questions: (a) What is the nature of the oscillations as seen by time-resolved cryo-EM? (b) Do microtubules disassemble by fraying protofilament fragments during oscillations at 37°C?

scholarly journals Alpha helical surfactant-like peptides self-assemble into pH-dependent nanostructures

Soft Matter ◽  
2021 ◽  
Vol 17 (11) ◽  
pp. 3096-3104
Author(s):  
Valeria Castelletto ◽  
Jani Seitsonen ◽  
Janne Ruokolainen ◽  
Ian W. Hamley
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Small Angle ◽  
Self Assembly ◽  
X Ray ◽  
Cryogenic Transmission Electron Microscopy ◽  
X Ray Scattering ◽  
Transmission Electron ◽  
Ph Dependent ◽  
Ray Scattering

A designed surfactant-like peptide is shown, using a combination of cryogenic-transmission electron microscopy and small-angle X-ray scattering, to have remarkable pH-dependent self-assembly properties.

scholarly journals Small angle x-ray scattering and electron microscopy of nanoparticles formed in an electrical arc

AIP Advances ◽  
2013 ◽  
Vol 3 (3) ◽  
pp. 032139 ◽  
Author(s):  
E. Carvou ◽  
J. L. Le Garrec ◽  
J. Pérez ◽  
J. Praquin ◽  
M. Djeddi ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Small Angle ◽  
X Ray ◽  
Electrical Arc ◽  
X Ray Scattering ◽  
Ray Scattering

Analysis of InGaN/GaN single quantum wells by X-ray scattering and transmission electron microscopy

2003 ◽  
Vol 240 (2) ◽  
pp. 297-300 ◽  
Author(s):  
T. M. Smeeton ◽  
M. J. Kappers ◽  
J. S. Barnard ◽  
M. E. Vickers ◽  
C. J. Humphreys
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Quantum Wells ◽  
Single Quantum ◽  
X Ray ◽  
X Ray Scattering ◽  
Transmission Electron ◽  
Ray Scattering

scholarly journals Structure of the Lassa Virus Nucleoprotein Revealed by X-ray Crystallography, Small-angle X-ray Scattering, and Electron Microscopy

2011 ◽  
Vol 286 (44) ◽  
pp. 38748-38756 ◽  
Author(s):  
Linda Brunotte ◽  
Romy Kerber ◽  
Weifeng Shang ◽  
Florian Hauer ◽  
Meike Hass ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Small Angle ◽  
Lassa Virus ◽  
X Ray ◽  
X Ray Crystallography ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Differential effects of early growth conditions on colour-producing nanostructures revealed through small angle X-ray scattering and electron microscopy

2020 ◽  
Vol 223 (18) ◽  
pp. jeb228387
Author(s):  
Katarzyna Janas ◽  
Anna Łatkiewicz ◽  
Andrew Parnell ◽  
Dorota Lutyk ◽  
Julia Barczyk ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Small Angle ◽  
Condition Dependence ◽  
Tail Feather ◽  
Blue Tit ◽  
X Ray ◽  
Stage Of Development ◽  
X Ray Scattering ◽  
Ray Scattering

ABSTRACTThe costs associated with the production and maintenance of colour patches is thought to maintain their honesty. Although considerable research on sexual selection has focused on structurally coloured plumage ornaments, the proximate mechanisms of their potential condition dependence, and thus their honesty, is rarely addressed, particularly in an experimental context. Blue tit (Cyanistes caeruleus) nestlings have ultraviolet (UV)–blue structurally coloured tail feathers, providing a unique opportunity for investigation of the causes of variation in their colour. Here, we examined the influence of early growing conditions on the reflectance and structural properties of UV–blue-coloured tail feathers of blue tit nestlings. We applied a two-stage brood size manipulation to determine which stage of development more strongly impacts the quality of tail feather colouration and microstructure. We used small-angle X-ray scattering (SAXS) and electron microscopy to characterise the nanoscale and microscale structure of tail feather barbs. Nestlings from the broods enlarged at a later stage of growth showed a sex-specific rectrix development delay, with males being more sensitive to this manipulation. Contrary to predictions, treatment affected neither the quality of the barbs’ nanostructures nor the brightness and UV chroma of feathers. However, at the microscale, barbs’ keratin characteristics were impaired in late-enlarged broods. Our results suggest that nanostructure quality, which determines the UV–blue colour in tail feathers, is not sensitive to early rearing conditions. Furthermore, availability of resources during feather growth seems to impact the quality of feather microstructure more than body condition, which is likely to be determined at an earlier stage of nestling growth.

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