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Motivation

Molecular structural analysis


Provide information about non-crystalline
samples
Macromolecular systems
Heterogeneous solutions

General X-ray Scattering

X-ray scattering are based up on the idea that elastic collisions occur
between the incoming wave and a particle, causing the reflected
waves to scatter in all directions
There will be constructive interference along certain angles, causing
peaks to present themselves .
Braggs law for simple scattering.
n = 2 dsin( )

Small Angles Scattering

Possible to study non-repeating structures


Smaller angle causes the scattering vectors modulus to become
dependent on the reflected angle in the form 2/. Since amplitude is
defined as 2/q, the amplitude is equal to /
x-rays interact with the electrons surrounding atoms
Inhomogeneties in the electron density will affect the scattering
pattern
Small angles (<10 degrees) are considered, these effects can be
observed and will provide information about the size and shape of
macromolecules in the sample

Small angle X-ray scattering


(SAXS)
Possible to study non-repeating structures
Small angles (<10 degrees) are considered, these effects
can be observed and will provide information about the
size and shape of macromolecules in the sample
The interaction between x-ray radiation and particles in
the bulk
The average size of illuminated particles are measured in
the bulk
The SAXS method is actually non-destructive, accurate
and minimum sample preparation
SAXS investigate the particle by difference in electron
density and surrounding material

The
whole volume of sample is investigated and so
average values of structure parameters are obtained
SAXS is sensitive to large particles as compared to
small ones
In order to obtain high-order SASX the linear ( )
absorption coefficient must be taken small
i.e.
d
Scattering pattern are usually presented as a function
of q
i.e.
q

process to determine structures is used

The Form Factor


The form factor, P(q), of a particle is
an interference pattern
Oscillation of form factor is typically
gives the particle shape
In practical application many
particles are illuminated at the same
time
Monodisperse sample (protein
solutions )
Polydisperse sample

Different particles to be
analysed

The other densed systems

The structure factor


The additional interference pattern
multiplies with the atomic factor of a
single particle is called the
structure factor S(q)
Contains information about the
positions of the particles with respect
to each other
The peaks in the structure factor
become more and more pronounced ,
when particles arrangements goes

It defines the relatonship


between
the positions of the particles

The SAXS Instruments


The basic components are
Source
Collimation system
Sample holder
Beam stopper
Detection system

Advantages and Disadvantages

Sample does not need to be crystallized


Samples requires very little preparation time
Allows for analysis of larger (m ass or size ) particles than many other
methods such as crystallography (5-25nm )
Loss Of Information
Inability To Control The Scattering Length Density Easily

Applications

Biological protein and rna analysis


Particularly Good At Resolving RNAprotein complexes
very highly useful in the analysis of
wet gels and xerogels in biochemistry

Conclusion

Provide s information about larger, less-ordered


structures
Highly useful tool, particularly in the biological sciences
When combined with other techniques for structural
analysis , a great deal of information can be obtained
through its application

Diluted systems-I

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