Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin

Julian C.H. Chen; Zoë Fisher; Andrey Y. Kovalevsky; Marat Mustyakimov; B. Leif Hanson; Vladimir V. Zhurov; Paul Langan

doi:10.1107/S1744309111051499

Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin

Julian C.H. Chen, Zoë Fisher, Andrey Y. Kovalevsky, Marat Mustyakimov, B. Leif Hanson, Vladimir V. Zhurov, Paul Langan

Biological and Environmental Systems Sci

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

The room-temperature (RT) X-ray structure of H/D-exchanged crambin is reported at 0.85 Å resolution. As one of the very few proteins refined with anisotropic atomic displacement parameters at two temperatures, the dynamics of atoms in the RT and 100 K structures are compared. Neutron diffraction data from an H/D-exchanged crambin crystal collected at the Protein Crystallo-graphy Station (PCS) showed diffraction beyond 1.1 Å resolution. This is the highest resolution neutron diffraction reported to date for a protein crystal and will reveal important details of the anisotropic motions of H and D atoms in protein structures.

Original language	English
Pages (from-to)	119-123
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	68
Issue number	2
DOIs	https://doi.org/10.1107/S1744309111051499
State	Published - Feb 2012

Keywords

H/D exchange
crambin
neutron diffraction
ultrahigh resolution

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10.1107/S1744309111051499

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Chen, J. C. H., Fisher, Z., Kovalevsky, A. Y., Mustyakimov, M., Hanson, B. L., Zhurov, V. V., & Langan, P. (2012). Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(2), 119-123. https://doi.org/10.1107/S1744309111051499

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title = "Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin",

abstract = "The room-temperature (RT) X-ray structure of H/D-exchanged crambin is reported at 0.85 {\AA} resolution. As one of the very few proteins refined with anisotropic atomic displacement parameters at two temperatures, the dynamics of atoms in the RT and 100 K structures are compared. Neutron diffraction data from an H/D-exchanged crambin crystal collected at the Protein Crystallo-graphy Station (PCS) showed diffraction beyond 1.1 {\AA} resolution. This is the highest resolution neutron diffraction reported to date for a protein crystal and will reveal important details of the anisotropic motions of H and D atoms in protein structures.",

keywords = "H/D exchange, crambin, neutron diffraction, ultrahigh resolution",

author = "Chen, {Julian C.H.} and Zo{\"e} Fisher and Kovalevsky, {Andrey Y.} and Marat Mustyakimov and Hanson, {B. Leif} and Zhurov, {Vladimir V.} and Paul Langan",

year = "2012",

month = feb,

doi = "10.1107/S1744309111051499",

language = "English",

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Chen, JCH, Fisher, Z, Kovalevsky, AY, Mustyakimov, M, Hanson, BL, Zhurov, VV & Langan, P 2012, 'Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 68, no. 2, pp. 119-123. https://doi.org/10.1107/S1744309111051499

Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin. / Chen, Julian C.H.; Fisher, Zoë; Kovalevsky, Andrey Y. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 68, No. 2, 02.2012, p. 119-123.

Research output: Contribution to journal › Article › peer-review

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T1 - Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin

AU - Chen, Julian C.H.

AU - Fisher, Zoë

AU - Kovalevsky, Andrey Y.

AU - Mustyakimov, Marat

AU - Hanson, B. Leif

AU - Zhurov, Vladimir V.

AU - Langan, Paul

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AB - The room-temperature (RT) X-ray structure of H/D-exchanged crambin is reported at 0.85 Å resolution. As one of the very few proteins refined with anisotropic atomic displacement parameters at two temperatures, the dynamics of atoms in the RT and 100 K structures are compared. Neutron diffraction data from an H/D-exchanged crambin crystal collected at the Protein Crystallo-graphy Station (PCS) showed diffraction beyond 1.1 Å resolution. This is the highest resolution neutron diffraction reported to date for a protein crystal and will reveal important details of the anisotropic motions of H and D atoms in protein structures.

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Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin

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