Protein crystallography with spallation neutrons

Benno P. Schoenborn; Paul Langan

doi:10.1107/S0909049503023902

Protein crystallography with spallation neutrons

Benno P. Schoenborn, Paul Langan

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

24 Scopus citations

Abstract

Spallation neutrons are ideal for diffraction studies of proteins and oriented molecular complexes. With spallation neutrons and their time dependent wavelength structure, one can select data with an optimal wavelength band and cover the whole Laue spectrum as time (wavelength) resolved diffraction data. This optimises data quality with best peak to background ratios and provides spatial and energy resolution to eliminate peak overlaps. Such a Protein Crystallography Station (PCS) has been built and tested at Los Alamos Neutron Science Centre. A partially coupled moderator is used to increase flux and data are collected by a cylindrical He detector covering 120° with 200mm height. The PCS is described along with some examples of data collected from proteins.

Original language	English
Pages (from-to)	80-82
Number of pages	3
Journal	Journal of Synchrotron Radiation
Volume	11
Issue number	1
DOIs	https://doi.org/10.1107/S0909049503023902
State	Published - Jan 1 2004
Externally published	Yes

Keywords

Enzyme mechanism
Neutron diffraction
PCS
Protein crystallography station

Access to Document

10.1107/S0909049503023902

Cite this

@article{c0ea46341f4e4351a00d24d06a88c22c,

title = "Protein crystallography with spallation neutrons",

abstract = "Spallation neutrons are ideal for diffraction studies of proteins and oriented molecular complexes. With spallation neutrons and their time dependent wavelength structure, one can select data with an optimal wavelength band and cover the whole Laue spectrum as time (wavelength) resolved diffraction data. This optimises data quality with best peak to background ratios and provides spatial and energy resolution to eliminate peak overlaps. Such a Protein Crystallography Station (PCS) has been built and tested at Los Alamos Neutron Science Centre. A partially coupled moderator is used to increase flux and data are collected by a cylindrical He detector covering 120° with 200mm height. The PCS is described along with some examples of data collected from proteins.",

keywords = "Enzyme mechanism, Neutron diffraction, PCS, Protein crystallography station",

author = "Schoenborn, {Benno P.} and Paul Langan",

year = "2004",

month = jan,

day = "1",

doi = "10.1107/S0909049503023902",

language = "English",

volume = "11",

pages = "80--82",

journal = "Journal of Synchrotron Radiation",

issn = "0909-0495",

publisher = "International Union of Crystallography",

number = "1",

}

TY - JOUR

T1 - Protein crystallography with spallation neutrons

AU - Schoenborn, Benno P.

AU - Langan, Paul

PY - 2004/1/1

Y1 - 2004/1/1

N2 - Spallation neutrons are ideal for diffraction studies of proteins and oriented molecular complexes. With spallation neutrons and their time dependent wavelength structure, one can select data with an optimal wavelength band and cover the whole Laue spectrum as time (wavelength) resolved diffraction data. This optimises data quality with best peak to background ratios and provides spatial and energy resolution to eliminate peak overlaps. Such a Protein Crystallography Station (PCS) has been built and tested at Los Alamos Neutron Science Centre. A partially coupled moderator is used to increase flux and data are collected by a cylindrical He detector covering 120° with 200mm height. The PCS is described along with some examples of data collected from proteins.

AB - Spallation neutrons are ideal for diffraction studies of proteins and oriented molecular complexes. With spallation neutrons and their time dependent wavelength structure, one can select data with an optimal wavelength band and cover the whole Laue spectrum as time (wavelength) resolved diffraction data. This optimises data quality with best peak to background ratios and provides spatial and energy resolution to eliminate peak overlaps. Such a Protein Crystallography Station (PCS) has been built and tested at Los Alamos Neutron Science Centre. A partially coupled moderator is used to increase flux and data are collected by a cylindrical He detector covering 120° with 200mm height. The PCS is described along with some examples of data collected from proteins.

KW - Enzyme mechanism

KW - Neutron diffraction

KW - PCS

KW - Protein crystallography station

UR - http://www.scopus.com/inward/record.url?scp=2142854125&partnerID=8YFLogxK

U2 - 10.1107/S0909049503023902

DO - 10.1107/S0909049503023902

M3 - Article

C2 - 14646140

AN - SCOPUS:2142854125

SN - 0909-0495

VL - 11

SP - 80

EP - 82

JO - Journal of Synchrotron Radiation

JF - Journal of Synchrotron Radiation

IS - 1

ER -

Protein crystallography with spallation neutrons

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this