TY - JOUR
T1 - Small-angle neutron scattering and contrast variation
T2 - A powerful combination for studying biological structures
AU - Heller, William T.
PY - 2010/11
Y1 - 2010/11
N2 - The use of small-angle scattering (SAS) in the biological sciences continues to increase, driven as much by the need to study increasingly complex systems that are often resistant to crystallization or are too large for NMR as by the availability of user facilities and advancements in the modelling of biological structures from SAS data. SAS, whether with neutrons (SANS) or X-rays (SAXS), is a structural probe of length scales ranging from 10 to 10 000 Å. When applied to biological complexes in dilute solution, it provides size and shape information that can be used to produce structural models that can provide insight into function. SANS enables the use of contrast-variation methods through the unique interaction of neutrons with hydrogen and its isotope deuterium. SANS with contrast variation enables the visual-ization of components within multisubunit complexes, making it a powerful tool for probing protein-protein and protein-nucleic acid complexes, as well as the interaction of proteins with lipids and detergents.
AB - The use of small-angle scattering (SAS) in the biological sciences continues to increase, driven as much by the need to study increasingly complex systems that are often resistant to crystallization or are too large for NMR as by the availability of user facilities and advancements in the modelling of biological structures from SAS data. SAS, whether with neutrons (SANS) or X-rays (SAXS), is a structural probe of length scales ranging from 10 to 10 000 Å. When applied to biological complexes in dilute solution, it provides size and shape information that can be used to produce structural models that can provide insight into function. SANS enables the use of contrast-variation methods through the unique interaction of neutrons with hydrogen and its isotope deuterium. SANS with contrast variation enables the visual-ization of components within multisubunit complexes, making it a powerful tool for probing protein-protein and protein-nucleic acid complexes, as well as the interaction of proteins with lipids and detergents.
UR - http://www.scopus.com/inward/record.url?scp=78049461183&partnerID=8YFLogxK
U2 - 10.1107/S0907444910017658
DO - 10.1107/S0907444910017658
M3 - Article
C2 - 21041939
AN - SCOPUS:78049461183
SN - 0907-4449
VL - 66
SP - 1213
EP - 1217
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 11
ER -