The use of neutron scattering to determine the functional structure of glycoside hydrolase

Akihiko Nakamura, Takuya Ishida, Masahiro Samejima, Kiyohiko Igarashi

Research output: Contribution to journalArticleScientificpeer-review

Abstract

Neutron diffraction provides different information from X-ray diffraction, because neutrons are scattered by atomic nuclei, whereas X-rays are scattered by electrons. One of the key advantages of neutron crystallography is the ability to visualize hydrogen and deuterium atoms, making it possible to observe the protonation state of amino acid residues, hydrogen bonds, networks of water molecules and proton relay pathways in enzymes. But, because of technical difficulties, less than 100 enzyme structures have been evaluated by neutron crystallography to date. In this review, we discuss the advantages and disadvantages of neutron crystallography as a tool to investigate the functional structure of glycoside hydrolases, with some examples.
Original languageEnglish
Pages (from-to)54-61
JournalCurrent Opinion in Structural Biology
Volume40
DOIs
Publication statusPublished - 2016
MoE publication typeA1 Journal article-refereed

Fingerprint

Glycoside Hydrolases
Neutrons
Crystallography
Hydrogen
Neutron Diffraction
Deuterium
Enzymes
X-Ray Diffraction
Protons
X-Rays
Electrons
Amino Acids
Water

Keywords

  • glycosidase
  • proton

Cite this

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title = "The use of neutron scattering to determine the functional structure of glycoside hydrolase",
abstract = "Neutron diffraction provides different information from X-ray diffraction, because neutrons are scattered by atomic nuclei, whereas X-rays are scattered by electrons. One of the key advantages of neutron crystallography is the ability to visualize hydrogen and deuterium atoms, making it possible to observe the protonation state of amino acid residues, hydrogen bonds, networks of water molecules and proton relay pathways in enzymes. But, because of technical difficulties, less than 100 enzyme structures have been evaluated by neutron crystallography to date. In this review, we discuss the advantages and disadvantages of neutron crystallography as a tool to investigate the functional structure of glycoside hydrolases, with some examples.",
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The use of neutron scattering to determine the functional structure of glycoside hydrolase. / Nakamura, Akihiko; Ishida, Takuya; Samejima, Masahiro; Igarashi, Kiyohiko.

In: Current Opinion in Structural Biology, Vol. 40, 2016, p. 54-61.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - The use of neutron scattering to determine the functional structure of glycoside hydrolase

AU - Nakamura, Akihiko

AU - Ishida, Takuya

AU - Samejima, Masahiro

AU - Igarashi, Kiyohiko

PY - 2016

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AB - Neutron diffraction provides different information from X-ray diffraction, because neutrons are scattered by atomic nuclei, whereas X-rays are scattered by electrons. One of the key advantages of neutron crystallography is the ability to visualize hydrogen and deuterium atoms, making it possible to observe the protonation state of amino acid residues, hydrogen bonds, networks of water molecules and proton relay pathways in enzymes. But, because of technical difficulties, less than 100 enzyme structures have been evaluated by neutron crystallography to date. In this review, we discuss the advantages and disadvantages of neutron crystallography as a tool to investigate the functional structure of glycoside hydrolases, with some examples.

KW - glycosidase

KW - proton

U2 - 10.1016/j.sbi.2016.07.014

DO - 10.1016/j.sbi.2016.07.014

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