iucr

commissions

principles
aperiodic crystals
biological macromolecules
crystal growth and characterization of materials
crystallographic computing
crystallographic nomenclature
crystallographic teaching
crystallography in art and cultural heritage
crystallography of materials
electron crystallography
high pressure
inorganic and mineral structures
international tables
journals
magnetic structures
mathematical and theoretical crystallography
neutron scattering
nmr crystallography
powder diffraction
quantum crystallography
small-angle scattering
structural chemistry
synchrotron and xfel radiation
xafs

congress

2021 iucr xxv
2017 iucr xxiv
2014 iucr xxiii
2011 iucr xxii
2008 iucr xxi
2005 iucr xx
2002 iucr xix
1999 iucr xviii
1996 iucr xvii
1993 iucr xvi
1990 iucr xv
1987 iucr xiv
1984 iucr xiii
1981 iucr xii
1978 iucr xi
1975 iucr x
1972 iucr ix
1969 iucr viii
1966 iucr vii
1963 iucr vi
1960 iucr v
1957 iucr iv
1954 iucr iii
1951 iucr ii
1948 iucr i

people

nobel prize

all
agre
anfinsen
barkla
boyer
w.h.bragg
w.l.bragg
brockhouse
de broglie
charpak
crick
curl
davisson
debye
deisenhofer
geim
de gennes
hauptman
hodgkin
huber
karle
karplus
kendrew
klug
kobilka
kornberg
kroto
laue
lefkowitz
levitt
lipscomb
mackinnon
michel
novoselov
pauling
perutz
ramakrishnan
roentgen
shechtman
shull
skou
smalley
steitz
sumner
thomson
walker
warshel
watson
wilkins
yonath

resources

commissions

aperiodic crystals
biological macromolecules
crystal growth and characterization of materials
crystallographic computing
crystallographic nomenclature
crystallographic teaching
crystallography in art and cultural heritage
crystallography of materials
electron crystallography
high pressure
inorganic and mineral structures
international tables
journals
magnetic structures
mathematical and theoretical crystallography
neutron scattering
NMR crystallography
powder diffraction
quantum crystallography
small-angle scattering
structural chemistry
synchrotron radiation
xafs

outreach

openlabs

calendar
Bruker OpenLab Congo-Brazzaville
LAAAMP Bruker OpenLab Benin
Bruker OpenLab Ghana
Malvern Panalytical OpenLab Turkey 2
Bruker OpenLab Côte d'Ivoire
LAAMP OpenLab Costa Rica
IUCr-IUPAP-ICTP OpenLab Senegal
Bruker OpenLab Cameroon
Rigaku OpenLab Bolivia
Bruker OpenLab Albania
Bruker OpenLab Uruguay 2
Rigaku OpenLab Cambodia 2
Bruker OpenLab Vietnam 2
Bruker OpenLab Senegal
PANalytical OpenLab Mexico 2
CCDC OpenLab Kenya
Bruker OpenLab Tunisia
Bruker OpenLab Algeria
PANalytical OpenLab Turkey
Bruker OpenLab Vietnam
Agilent OpenLab Hong Kong
PANalytical OpenLab Mexico
Rigaku OpenLab Colombia
grenoble-darmstadt
Agilent OpenLab Turkey
Bruker OpenLab Indonesia
Bruker OpenLab Uruguay
Rigaku OpenLab Cambodia
PANalytical OpenLab Ghana
Bruker OpenLab Morocco
Agilent OpenLab Argentina
Bruker OpenLab Pakistan

Since the discovery of the diffraction of X-rays by crystals just over 100 years ago, X-ray diffraction as a method of structure determination has dominated structural research in materials science and biology. However, many of the most important materials whose structures remain unknown do not readily crystallize as three-dimensional periodic structures. Crystallization can also alter the properties of the material to be studied: a crystallized protein may not function in the way that it would in its natural state, and confining nanostructures such as carbon nanotubes within a crystal lattice can also alter their behaviour.

In the March issue of *Acta Crystallographica Section A*, Jüstel, Friesecke and James propose a new method for studying these kinds of structures, using twisted X-rays [*Acta Cryst*. (2016). A**72**, doi:10.1107/S2053273315024390]. They show that the key to obtaining diffraction data from non-crystalline but symmetric structures, such as helices, lies in matching the symmetry of the incoming radiation to the symmetry of the structure to be studied.

The interesting resonance effects of twisted waves with helical structures suggests that this could be a promising new method for structure determination: send twisted X-rays onto a helical structure, align the waves, the structure and the detector axially, and the outgoing radiation shows sharp, discrete peaks as the incoming wavelength and the amount of twist are varied. Structure prediction from the diffraction pattern then works in exactly the same way as in the case of crystals. Using computer simulations, the authors show that the accuracy of a structure determined using twisted X-rays would be comparable to that obtained by 'classical' X-ray methods.

Remarkably, the method can applied to some of the most important structures in biology and a striking number of the structures that are emerging in nanoscience: buckyballs and many fullerenes, the parts of many viruses, actin, carbon nanotubes (all chiralities), graphene and a large collection of other two-dimensional structures, such as the currently important structures of black phosphorus and the dichalcogenides.

Now someone just has to design the machine to put the twist into the X-rays!

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