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Title: Powder diffraction studies on proteins : An overview of data collection approaches.

Abstract

Following the seminal work of Von Dreele, high quality powder X-ray diffraction studies on proteins are being established as a valuable complementary technique to single-crystal measurements. Several studies using a variety of experiments approaches have been reported in the literature, including high-resolution studies employing parallel beam geometry and high intensity measurements using position sensitive detectors. The choice of the optimum instrumental configuration depends on a number of competing factors such as the amount of sample available, its radiation sensitivity, and the quality of the data required for data analysis, e.g. angular resolution, the extent of the data in d-spacing, or the number of patterns required to explore the protein's behaviour at different temperatures, or under different crystallisation conditions, etc. Here we discuss several advantages and disadvantages of different data collection methods followed for selected examples of small proteins.

Authors:
; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
971135
Report Number(s):
ANL/XSD/CP-58081
TRN: US201003%%587
DOE Contract Number:
DE-AC02-06CH11357
Resource Type:
Conference
Resource Relation:
Journal Name: Z. Kristallogr.; Journal Volume: 26; Journal Issue: 2007; Conference: European Powder Diffraction Conference (EPDIC-10); Sep. 1, 2006 - Sep. 4, 2006; Geneva, Switzerland
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; CONFIGURATION; DATA ANALYSIS; DIFFRACTION; GEOMETRY; POSITION SENSITIVE DETECTORS; PROTEINS; RADIATIONS; RESOLUTION; SENSITIVITY; X-RAY DIFFRACTION

Citation Formats

Margiolaki, I., Wright, J. P., Fitch, A. N., Fox, G. C., Labrador, A., Von Dreele, R. B., Miura, K., Gozzo, F., Schiltz, M., Besnard, C., Camus, F., Pattison, P., Beckers, D., Degen, T., X-Ray Science Division, European Synchrotron Radiation Facility, Japan Synchrotron Radiation Research Inst., Swiss Light Source, Ecole Polytechnique Federale de Lausanne, and PANalytical. Powder diffraction studies on proteins : An overview of data collection approaches.. United States: N. p., 2007. Web. doi:10.1524/zksu.2007.2007.suppl_26.1.
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Margiolaki, I., Wright, J. P., Fitch, A. N., Fox, G. C., Labrador, A., Von Dreele, R. B., Miura, K., Gozzo, F., Schiltz, M., Besnard, C., Camus, F., Pattison, P., Beckers, D., Degen, T., X-Ray Science Division, European Synchrotron Radiation Facility, Japan Synchrotron Radiation Research Inst., Swiss Light Source, Ecole Polytechnique Federale de Lausanne, & PANalytical. Powder diffraction studies on proteins : An overview of data collection approaches.. United States. doi:10.1524/zksu.2007.2007.suppl_26.1.
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Margiolaki, I., Wright, J. P., Fitch, A. N., Fox, G. C., Labrador, A., Von Dreele, R. B., Miura, K., Gozzo, F., Schiltz, M., Besnard, C., Camus, F., Pattison, P., Beckers, D., Degen, T., X-Ray Science Division, European Synchrotron Radiation Facility, Japan Synchrotron Radiation Research Inst., Swiss Light Source, Ecole Polytechnique Federale de Lausanne, and PANalytical. Mon . "Powder diffraction studies on proteins : An overview of data collection approaches.". United States. doi:10.1524/zksu.2007.2007.suppl_26.1.
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@article{osti_971135,
title = {Powder diffraction studies on proteins : An overview of data collection approaches.},
author = {Margiolaki, I. and Wright, J. P. and Fitch, A. N. and Fox, G. C. and Labrador, A. and Von Dreele, R. B. and Miura, K. and Gozzo, F. and Schiltz, M. and Besnard, C. and Camus, F. and Pattison, P. and Beckers, D. and Degen, T. and X-Ray Science Division and European Synchrotron Radiation Facility and Japan Synchrotron Radiation Research Inst. and Swiss Light Source and Ecole Polytechnique Federale de Lausanne and PANalytical},
abstractNote = {Following the seminal work of Von Dreele, high quality powder X-ray diffraction studies on proteins are being established as a valuable complementary technique to single-crystal measurements. Several studies using a variety of experiments approaches have been reported in the literature, including high-resolution studies employing parallel beam geometry and high intensity measurements using position sensitive detectors. The choice of the optimum instrumental configuration depends on a number of competing factors such as the amount of sample available, its radiation sensitivity, and the quality of the data required for data analysis, e.g. angular resolution, the extent of the data in d-spacing, or the number of patterns required to explore the protein's behaviour at different temperatures, or under different crystallisation conditions, etc. Here we discuss several advantages and disadvantages of different data collection methods followed for selected examples of small proteins.},
doi = {10.1524/zksu.2007.2007.suppl_26.1},
journal = {Z. Kristallogr.},
number = 2007,
volume = 26,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}
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Conference:
DOI:  10.1524/zksu.2007.2007.suppl_26.1
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