X-Ray Microscopy

Related terms:

Nanowire, Electron Microscopy, Behavior as Electrode, Wavelength, Soft X-Ray,

Aerosol, Transmission Electron Microscopy

View all Topics

Learn more about X-Ray Microscopy

Chemical Imaging Analysis

Freddy Adams, Carlo Barbante, in Comprehensive Analytical Chemistry, 2015

High-Resolution Transmission X-ray Microscopy

Transmission X-Ray Microscopy (TXM) is based on the principle of projecting onto a
detector a magnified image of the sample obtained with a small divergent source. To
this aim, the nearly parallel beam of the synchrotron is focussed on a small secondary
source in front of the sample. In a typical TXM synchrotron setup the X-ray beam is
first focussed with mirrors, and the energy is tuned with a monochromator. TXM
optics generally consist of a condenser based on KB mirrors, Fresnel zone plate
or elliptical capillary to focus light upon the sample, and a zone plate to magnify
the image onto a 2-D pixellated detector using absorption or phase contrast. In
numerous current designs spatial resolution is about 30 nm with imaging times of
about 1–100 s per image, depending on source intensity and contrast in the sample.

> Read full chapter

X-Ray Fluorescence and Emission | Syn-

chrotron X-Ray Fluorescence☆
Freddy C. Adams, in Encyclopedia of Analytical Science (Third Edition), 2019
Abstract
X-rays have the advantage that they have a short wavelength and can penetrate
through thick samples. Many of the X-ray microscopy techniques that provide
the greatest sensitivity and specificity for trace metal analysis are emerging at
synchrotron X-ray facilities. The extremely high flux available across a wide range
of soft and hard X-rays, combined with state-of-the-art focusing techniques and
ultra-sensitive detectors, makes it viable to undertake direct imaging of elemental
composition in various materials. Methods covered in this review include X-ray
fluorescence for elemental imaging, X-ray absorption spectrometry for speciation
imaging, X-ray diffraction for structural imaging, and phase contrast for enhanced
contrast imaging. Two- and three-dimensional (confocal and tomographic) imaging
methods are considered.

> Read full chapter

Chemical Imaging Analysis

Freddy Adams, Carlo Barbante, in Comprehensive Analytical Chemistry, 2015

3.5.7 X-ray Analysis at Third-Generation SR Sources

The unique properties of SR generated by third-generation sources coupled with
state-of-the-art X-ray optical elements/detectors offer new possibilities in various
X-ray microscopy and microprobe methods, in terms of achievable spatial resolution
and sensitivity. In addition to the high intensity, high degree of polarisation and
energy tenability of SR light, another valuable feature is its capability to provide high-
ly spatially/temporally coherent X-ray illumination. Due to their high penetration
power, X-rays also enable the study of bulk regions of thick samples in their natural
environment (air, water, etc.). Advantages and disadvantages are summarised in
Table 3.3.

Table 3.3. Advantages/Disadvantages of Synchrotron X-ray Analysis

Analytical characteristics, (sensitivity, accuracy, Accessibility of SR sources, difficult, competitive,

multielement, etc.) slow access
Different sources of information, (elemental, spe- No routine applications, important topics, novel
ciation, structural) science, etc.
Transmission of X-rays, (2-D, 3-D analysis, use in
air, etc.)
Quick pace of development, (spatial analysis, sensitivity, etc.)
Coherence and imaging
> Read full chapter

X-ray absorption fine structure in the

study of semiconductor heterostruc-
tures and nanostructures
Federico Boscherini, in Characterization of Semiconductor Heterostructures and
Nanostructures, 2008

2.4.3 Micro-XAFS
As brighter synchrotron sources have become available it has become possible to
obtain smaller focal spot sizes and to design instruments capable of increasingly
higher spatial resolution. In fact, the field of X-ray microscopy has progressed
very rapidly in recent years; lateral resolutions of the order of 10 nm have been
obtained with photoelectron imaging techniques, e.g., the photo emission electron
microscope or PEEM (see Locatelli et al. [100] for an example of a spectromicroscopy
beamline using photoelectron imaging, and Ratto et al. [100] for an example of
application to Ge dots on Si).

There is a great interest in performing XAFS with high lateral resolution (micro-XAFS)
as it allows a new level of description of heterogeneous samples, combining mi-
croscopy with the atomic-scale structural information obtainable from XAFS; with
sufficiently small focal spots the local atomic environment of single nanostructures
might be determined. The challenge is to record XAFS spectra free of systematic
errors and with sufficiently good signal-to-noise ratio. At present, XAFS spectra can
be recorded with spot sizes of the order of a few square micrometers, for example,
on the ID22 beamline [101] of the ESRF or on the LUCIA beamline [102] of the SLS;
micro-XAFS is often complemented with microfluorescence mapping. Applications
of micro-XAFS to semiconductors have been relatively limited so far, but it is expect-
ed much progress will be made in this field. Micro-XAFS is particularly useful when
the samples investigated exhibit lateral inhomogeneities and it is not surprising
that many applications in the field of semiconductors have been on samples the
growth of which has yet to be optimized, for example DMSs based on GaN, as
will be discussed in Section 3. In several synchrotron radiation laboratories, efforts
are on the way to combine the information which can be derived from XAFS with
the nanometer-level lateral resolution which can be obtained by using atomic force
microscope tips [103]. While photon-based techniques might maybe never reach the
sub-angstrom spatial resolution obtainable in electron microscopy, the advances in
recent years have been really dramatic as they involve many orders of magnitude
improvement in spatial resolution. In the future, micro-XAFS will certainly become
a powerful tool in materials science, complementing spatially averaged techniques
which have been the key to the success and widespread use of X-rays for structural
determination.

> Read full chapter

RO Membrane Characterization
Ahmad Fauzi Ismail, ... Takeshi Matsuura, in Reverse Osmosis, 2019

3.3.6 Scanning Transmission X-ray Microscopy (STXM)

This can be used for examining hydrated biofilms (in RO fouling) due to the ability of
soft X-rays to penetrate water. Lawrence et al. [45] have used scanning transmission
X-ray microscopy (STXM), confocal laser scanning microscopy (CLSM), and TEM to
map the distribution of macromolecular subcomponents (e.g., polysaccharides, pro-
teins, lipids, and nucleic acids) in a biofilm and demonstrated that this combination
of multi-microscopy analysis can be used to create a detailed correlative map of
biofilm structure and composition. Thus, it can help to understand the chemistry of
fouling.

> Read full chapter

Some Miscellaneous Speculations

STEPHEN HYDE, ... SVEN LIDIN, in The Language of Shape, 1997

8.2.5 Muscle contraction

Myosin and actin are remarkable molecules, responsible for mobility in animals,
from amoeba to mammals. The hexagonal arrangement of the helical structures of
actin, myosin and the interpenetrating actin/myosin regions have been well char-
acterised from ultrastructural X-ray and electron microscopy studies. The hexagonal
cross-section is shown in Fig. 8.8. The structure is highly hydrated, with short-range
disorder combined with long-range order, which is similar to that in lipid systems.
The liquid-crystalline character is obvious from the viscoelastic rheological behaviour
and the optical birefringence. Despite the fact that the liquid-crystalline nature of the
muscle cell was pointed out by Lehmann at the beginning of this century, it seems
to have been neglected since then. As will be demonstrated below, it is especially
fruitful to consider the long-range periodicity of the structure to understand the
mechanisms involved in the contraction process.

Figure 8.8. Cross-section of the hexagonal arrangement of myosin (large circles) and
actin (small filled circles) in the muscle cell.

The molecular events underlying the contraction of muscle involves release of

calcium ions from the sarcoplasmatic reticulum as a result of acetylcholine release
from the corresponding nerve. Binding of ATP to the myosin heads is the first step
in the cycle of relative movement of actin/myosin. Following that, ATP-myosin heads
bind to actin molecules, dephosphorylation (the myosin head also functions as an
ATP-ase) and dissociation of the actin-myosin complex and of ADP from the myosin.
A force, resulting in the relative movement of myosin/actin is produced during these
steps, and the cycles are repeated about 50 times per second. The movement in each
cycle is about 10 nm.

“Free” myosin molecules associate spontaneously into bundles like those in the
muscle cell. The molecule is one of the longest known in nature (155 nm) with
twin-heads extending from the bundle in a helical fashion and the tail consisting
of a coiled coil double helix (pitch 7.5 nm). The distal part of this tail (110 nm) forms
the bundle and the heads are pointed outwards by a “hinge” (45 nm). The period
between the heads along the axis of a bundle is 14.3 nm.

It should be remarked, however, that calcium plays a crucial role in the actin-myosin
association/dissociation process. Calcium has a binding site on troponin, located on
the surface of the actin thread, and binding of calcium triggers the contraction cycle.
(Without calcium there is no association whatsoever.)

The most intriguing problem in this process is the mechanism behind the produc-
tion of force and motion from ATP-hydrolysis. It is of interest here to cite Pollard [21]:
“Those who believe the lovely textbook drawings that depict tilting crossbridges pulling
actin filaments past myosin thick filaments may even think that the problem has been
solved. Much has been learned, but the secrets of cross-bridge motion have resolutely
evaded the efforts of a generation of biophysicists and biochemists”.
Various theories have been introduced to explain the relative movement. Huxley
proposed that the myosin head changed its orientation after binding to actin (the
“rotating-head” model). According to the helix-coil transition, the normally -helical
coiled-coil structure “melts” to a random coil conformation, which implies a reduc-
tion in length. Movements of the myosin tails, as well as conformation changes of
the actin have also been considered. It now seems clear, however, that the force
production takes place in or very near the myosin heads [22]. Furthermore, among
the three different states of myosin - empty actin site, ATP bound to the actin site
and ADP-Pi bound to the actin site - all of which can either be free or bound to actin,
there is evidence that the motion is produced by dissociation by the products of ATP
hydrolysis.

Rigor cross-bridges are considered to represent the final conformation of the

ATP-driven contraction. A detailed three-dimensional picture of the rigor structure
of actin and myosin in insect flight muscles has been recently reported [22]. It
resembles a (principally) hyperbolic surface, defining the interface between actin as
well as myosin and the water medium. Furthermore, different conformations of the
myosin heads seem to reflect different states of the contraction cycle.

A structural dilemma lies in combining a phase concept of the molecular arrange-

ment with the molecular description of the contraction process. It is known that
the movements of different myosin heads on a particular myosin thread occur
asynchronously, which is evident for example, from X-ray diffraction experiments.
That means that a force is generated constantly with time. The coordination of
movement between every muscle cell (down to the individual actin/myosin molecule)
is controlled by the excitation via the tubuli system, which is a cubosome type of
membrane system, described in the previous chapter.

The interpenetrating structure (Fig. 8.9) wherein the mobility originates can be
described by the Q* surface (discussed above). The long-range periodicity, which
is a consequence of such a structural description, is relevant to understand the
cooperativity and the requirement of synchronisation of the movement of the in-
dividual myosin/actin. The phase/curvature approach to the structure of the muscle
cell outlined here not only has a didactic value, but adds a new dimension to the
discussion of function mechanisms.
Figure 8.9(a). The rectangular nets forming the Q* surface. Two such nets seen along
the c-axis are shown above (distance c/6) (broken and full lines). (b) The hexagonal
network, characteristic of the desmin network.

The muscle cell contains predominantly water, and the organisation of the self-as-
sembled actin and myosin threads, which is based on hydrophobic interaction,
must follow the general principles outlined in Chapter 4. In contrast to the simple
liquid-crystalline systems considered there, we do not know the curvature of the
interface. A description based on surfaces with constant average curvature nonethe-
less appears the most reasonable line of attack, due to the analogy with other
self-assembled systems.

The myosin heads are helically distributed and the actin molecules form helical
double strands. There are also additional helical elements attached to the actin
threads, but they can be ignored in this context. The cross-sectional arrangement
of actin and myosin shown in Fig. 8.8 is consistent with the Q* surface. The myosin
molecules are centred on the 62 axes and actin on 31 axes, which occur in the
proportion 2:1. The Q* surface partitioning of space into helical channel systems cor-
responds to the position of the myosin threads. There is thus no connection between
adjacent channel systems, i.e. between neighbouring myosin threads. To understand
the connections between these channels, we can consider the rectangular nets,
which span this surface, shown in Fig. 8.9. The channels exhibit four-coordination;
alternatively we can regard the units as four-armed.

Two of these directions correspond to up and down along the myosin thread, and
the connections in the two lateral directions are also directed upwards and down-
wards. It is natural then to relate these four-coordinated channel regions of the Q*
surface to the myosin heads. Thus the possible connections via the 31-centred actin
threads of myosin threads have only two directions, which fulfil the crystallographic
symmetry of the surface. It is proposed here that these two directions correspond
to the initial direction of the myosin head before movement and the end direction
after movement, respectively. In this model of the contraction, the time-phase of
mobility represents a transient disorder condition of adjacent structure elements,
whereas the structure as a whole fulfils the required crystallographic symmetry. If
the individual molecular conformational changes must be accommodated within
the periodicity of the surface, the necessary perfect long-range synchronisation of
mobility over the entire muscle seems a natural consequence.

There is a further interesting structural feature of the muscle periodicity. The actin
threads in the opposite two directions of the perpendicular cross-section are linked
by the so-called “desmin” network, containing a rectangular cross-section. The
change from a rectangular to a hexagonal arrangement can take place continuously
between two surfaces produced by the same network, shown in Fig. 8.9(b). If the
adjacent networks are not twisted we obtain the rectangular surface, which can go
over to the Q* surface on twisting.

There is an important difference between the macroscopic actin/myosin structure in

muscle cells discussed above and the separate actin/myosin threads involved in the
locomotion of individual cells. This form of myosin (myosin I) is also quite different,
with one head instead of two as in muscle cells (myosin II), further it lacks a tail.
Another interesting property of myosin I is its membrane association: it can even
bind to phospholipid vesicles via anionic phospholipids [23].

Genetic engineering has recently provided a promising approach to the under-

standing of these functions. A myosin head fragment has been expressed [24] that
was found to display actin-activated ATP activity. Future results should improve our
understanding of this crucial physico-chemical process.

> Read full chapter

X-ray microtomography for materials

characterization
R. Hanke, ... S. Zabler, in Materials Characterization Using Nondestructive Evalua-
tion (NDE) Methods, 2016

3.2.1 X-ray microfocus tubes

The development of microfocus X-ray technology started in the late 1970s. Today, for
modern microfocus X-ray tubes, the progress in development results at focal spot
sizes down to 0.4 μm and thus enables high resolution direct magnification X-ray
microscopy by the use of such microfocus tubes as a source of radiation.

In this context, it is important to note that in fact radioscopic image resolution is

directly related to the tube's focal spot size and is of about the same order of mag-
nitude, whereas CT resolution in practice is in the best case the same as the spatial
resolution of a single projection. Usually, it is slightly worse than that due to the
additional limitations encountered with CT measurements, like long-term reliability
of focal spot size and position, inaccuracies of the mechanical manipulation system,
and stability of the imaging detector's calibration.

The characterization of microfocus X-ray tubes mainly is based on spot size mea-
surement. Even though significant progress has been made in decreasing spot
sizes below 1 μm, there are still no standardized methods for determination of focal
spot sizes smaller than 5 μm. The currently applied measurement procedures in
the submicron regime are based on test patterns, eg, JIMA “RT-RC 02” (cf. Fig. 3.2)
or the Siemens star-pattern used by companies like Carl Zeiss (formerly XRadia),
providing finest periodic structures of discrete or continuously decreasing size.
Some representative experimental results on this topic will be discussed in more
detail in Section 3.7 of this chapter.

Figure 3.2. Focal spot determination using a JIMA “RT-RC 02” resolution test pat-
tern. Highly magnified radiograph of pattern (left), enlarged view on the 1 μm
pattern (middle), extracted profile from the 1 μm structure (right).

Further details on the different determination methods can be found at (Salamon

et al., 2008a,b). The latest developments in standard microfocus X-ray technology are
related to higher stability of the focal spot position based on internal cooling of the
focusing device reducing the thermal elongation due to a temperature gradient of
approximately 60°C between standby and focused scan mode. Detailed information
about state of the art (design, function and characteristics like focal spot size, energy
range, power, etc.) can be read, eg, in Salamon et al. (2008a,b, 2009).

Advanced developments toward lab-based real nanometer-focus X-ray sources cur-

rently follow two approaches of new X-ray target conceptions. On the one hand,
there are new liquid metal jet targets (LMJ), generating high brilliance in the low en-
ergy region between 7 and 20 keV, with the gallium's K –line at 9.24 keV (cf. Fig. 3.3,
right (Otendal, 2006; Vogel, 2015; Hemberg et al., 2003)). On the other hand,
new needle or pin targets realize focal spot sizes down to 50 nm in combination
with electron focusing optics of a latest generation's electron microscope and thus
enabling magnification factors up to M = 1000 (Stahlhut et al., 2013, 2014).
Figure 3.3. Left: illustration of the gallium–indium metal jet, which allows for a
variable focal spot size and very high brilliance at the same time (Courtesy Excillum).
Application areas are essentially plastic materials and biological samples. Currently,
a spot size of around 80 μm by 20 μm can be achieved. Right: typical X-ray spectrum
resulting from an alloy of 69% gallium, 22% indium, 9% tin with 70 keV energy of
the incident electrons. The maximum tube voltage available is 160 kV in this case.

LMJ-based CT setups, in combination with advanced detector technology (high

speed or high resolution), can be used for materials characterization both in terms
of dynamic material analysis as well as structure characterization, respectively (-
Fig. 3.4). Moreover, the high brilliance in combination with stabilized manipulation
systems allows even phase contrast imaging or the application of focusing devices
(refractive lenses, zone plates, etc.) in laboratory environments within reasonable
measuring time (Zabler et al., 2012).

Figure 3.4. Wood cell structure as an example of a CT with a liquid metal jet X-ray
source.

Courtesy Balles, A. University of Würzburg, Germany.

To further reduce the focal spot size toward the nanometer-focus range—compared
to state-of-the-art microfocus X-ray tubes, which are based on transmission target-
s—a new pin target concept is realized inside an electron microscope (cf. Figs. 3.5
and 3.6). Especially produced needles, made of molybdenum or tungsten (Stahlhut,
2012) with tips in the range of about 50 nm will be placed directly into the electron
beam and thus produce X-rays with a focal spot size, limited only by the diameter of
the metal tip.

Figure 3.5. Upgrade of an electron microscope: sketch (left). Sample and X-ray

source are inside of the microscope's vacuum vessel (center). The extremely small
needle-targets are produced by electrochemical etching, tip size below 100 nm
(right).

Figure 3.6. Highest resolution achieved by nanometer imaging: the radiographic

resolution achieved is less than 100 nm by phase contrast. Thereby the sample size
must not be larger than 100 μm. Projection radiography were taken to prepare 3-D
imaging of an AlGeSi alloy; blue arrow: 500 nm wave-like surface details; red arrows:
hairline cracks down to 100 nm; Acquisition parameters 120 min exposure, 30 kV
tungsten X-ray spectrum, directly converting CdTe sensor with 1000 μm sensitive
layer and 55 μm pixel size.

Courtesy Stahlhut, P. University of Würzburg, Germany.

> Read full chapter

Volume II
Anthony D. Rollett, Katayun Barmak, in Physical Metallurgy (Fifth Edition), 2014

11.3.3 Differential Aperture X-ray Microscopy

The restriction to surface characterization with conventional laboratory-scale X-ray
sources is removed by using a synchrotron source of X-rays, which provides higher
energies and substantially higher intensities. The best known of these is the differ-
ential aperture X-ray microscopy (DAXM) method pioneered by the group at Oak
Ridge (Ice and Larson, 2000). In basic terms, polychromatic synchrotron radiation
is extracted from the accelerator in the energy range 8–22 keV. The experiments are
conducted at the Advanced Photon Source at Argonne National Laboratory. Note
that the intensity is finite over a range of wavelength so that the Laue technique can
be used, that is one diffraction pattern per point (in contrast to the some of the other
methods to be described). This gives an effective penetration up to 100 microns,
depending of course on the absorption coefficient of the material. Combinations
of mirrors and lenses are used to collimate the beam onto the specimen surface.
The high intensity shortens the time required to accumulate a diffraction pattern at
each point and the small spot size permits high spatial resolution. Crucially, however,
the provision of a wire, made of platinum or tungsten to have high absorption, that
passes between the specimen and the detector provides depth information. Figure 9
shows the geometry of the method, which explains that correlating which diffraction
spots weaken depending on the position of the wire allows the depth position of
the diffracting material to be resolved. The method is a differential aperture method
because it is equivalent in some sense to a pinhole camera but the moving wire
differentiates between one location and another as it blocks diffracted beams from
reaching the detector. Notwithstanding the high resolution and high orientation
accuracy achieved with this technique, it remains a near-surface method because of
the limited penetrating power of the X-rays in the energy range that is feasible for the
method, that is 22 keV. The DAXM method has the ability to map out orientations
in 3D with high enough spatial resolution that dislocation structures can be imaged
and quantified. This in turn allows the dislocation network to be analyzed in terms
of GND content (Yang et al., 2004a,b).
Figure 9. Diagram of the technique used to scan a highly absorbing wire over a
sample surface and block diffracted beams in a known sequence. This permits spatial
information to be obtained from the illuminated spot (Larson et al., 2002).

> Read full chapter

X-Ray Absorption Fine Structure in the

Study of Semiconductor Heterostruc-
tures and Nanostructures
F. Boscherini, in Characterization of Semiconductor Heterostructures and Nanos-
tructures (Second Edition), 2013

2.4.3 Micro-XAFS
One of the consequences of the orders-of-magnitude increase in the brightness of
synchrotron sources has been the possibility of obtaining smaller focal spot sizes
and to design instruments capable of increasingly higher spatial resolution. In fact,
the field of X-ray microscopy has progressed very rapidly in recent years; lateral
resolutions of the order of 10 nm can be obtained nowadays.

There is a great interest in performing XAFS with high lateral resolution (micro-XAFS)
since it allows a new level of description of heterogeneous samples, combining
microscopy with the atomic-scale structural information obtainable from XAFS; with
sufficiently small focal spots the local atomic environment of single nanostructures
might be determined. For details and up-to-date references the reader is referred to
chapter 9 by Martinez-Criado et al. [49]. Applications of micro-XAFS to semiconduc-
tors have been relatively limited so far, but it is expected they will be more numerous
in the future. Micro-XAFS is particularly useful when the samples investigated
exhibit lateral inhomogeneities and it is not surprising that many applications in
the field of semiconductors have been on samples the growth of which has yet to
be optimized, for example dilute magnetic semiconductors based on GaN, as will be
discussed in section 3. While photon-based techniques might maybe never reach the
sub-angstrom spatial resolution obtainable in electron microscopy, the advances in
recent years have been really dramatic since they involve many orders of magnitude
improvement in spatial resolution. In the future, micro-XAFS will certainly become
a powerful tool in materials science, complementing spatially averaged techniques
which have been the key to the success and widespread use of X-rays for structural
studies.

> Read full chapter

Laser spectroscopy for medical applica-

tions
S. Svanberg, in Laser Spectroscopy for Sensing, 2014

14.7.6 Super-resolution microscopy techniques

The spatial resolution of a microscope is limited by the wave nature of light, and,
according to the Abbe criterion, a resolution better than about half the wavelength
cannot be achieved, i.e. about 300 nm in the visible region. That is the reason why
X-ray microscopy imaging techniques have been developed.92 Another approach
has been to use electrons, which, as discussed in Section 14.1, also have a wave
nature, with wavelengths down to sub nm.93,94 Resolution in the optical regime can
be slightly improved by using two-photon absorption fluorescence spectroscopy.95
Since the resulting intensity is quadratically dependent on the light intensity, most
of the light comes from the area of highest intensity in a tightly focused beam. The
effective focal spot then becomes smaller and resolution is improved.

Recently, the limitations of the Abbe criterion for resolution in the visible have been
seriously challenged, and, in fact, several super-resolution techniques have been
developed. The first of these techniques is Stimulated Emission Depletion (STED),
which operates in fluorescence.96,97 The light emanates from the primarily focused
beam. However, by adding a donut-shaped beam which depletes the excited state
due to stimulated emission, the fluorescence can be limited to the center of the
donut, taking advantage of the non-linearity in the saturation process. In this way
a spatial resolution down to about 20 nm has been achieved. Figure 14.8 illustrates
the principles of STED. Similar non-linearities can be used in the frequency domain
to achieve a spectral resolution below the natural radiation width limit.99,100
 14.8. (a–d) Principles of STED, resolution improvement, and illustration of images.

Source: From Westphal and Hell.98

A further class of super-resolution methods rely on single-molecule fluorescence

detection. Marker molecules attach to structures on the nm scale and give rise to
fluorescence. The resulting light spot is again limited by the Abbe criterion. However,
if the molecules are switchable from a bright and a dark state, and a given molecule
can be made to emit many photons while the neighboring molecules do not emit,
the center of the emission spot from a single molecule can be determined much
more accurately than the position of an individual photon. The other molecules are
later in turn switched on to emit. By plotting the center location of the molecules,
a high spatial confinement, far below the diffraction limit, has been achieved. The
technique is referred to as Stochastic Optical Reconstruction Microscopy (STORM);-
101,102 a related technique is PALM (Photoactivated Localization Microscopy).103

> Read full chapter

ScienceDirect is Elsevier’s leading information solution for researchers.

Copyright © 2018 Elsevier B.V. or its licensors or contributors. ScienceDirect ® is a registered trademark of Elsevier B.V. Terms and conditions apply.