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Neutron protein crystallography

Abstract

X-ray diffraction of single crystal has enriched the knowledge of various biological molecules such as proteins, DNA, t-RNA, viruses, etc. It is difficult to make structural analysis of hydrogen atoms in a protein using X-ray crystallography, whereas neutron diffraction seems usable to directly determine the location of those hydrogen atoms. Here, neutron diffraction method was applied to structural analysis of hen egg-white lysozyme. Since the crystal size of a protein to analyze is generally small (5 mm{sup 3} at most), the neutron beam at the sample position in monochromator system was set to less than 5 x 5 mm{sup 2} and beam divergence to 0.4 degree or less. Neutron imaging plate with {sup 6}Li or Gd mixed with photostimulated luminescence material was used and about 2500 Bragg reflections were recorded in one crystal setting. A total of 38278 reflections for 2.0 A resolution were collected in less than 10 days. Thus, stereo views of Trp-111 omit map around the indol ring of Trp-111 was presented and the three-dimensional arrangement of 696H and 264D atoms in the lysozyme molecules was determined using the omit map. (M.N.)
Authors:
Niimura, Nobuo [1] 
  1. Japan Atomic Energy Research Inst., Tokai, Ibaraki (Japan). Tokai Research Establishment
Publication Date:
Oct 01, 1998
Product Type:
Conference
Report Number:
JAERI-Conf-98-015; CONF-9711223-
Reference Number:
SCA: 665100; PA: JPN-99:002207; EDB-99:039289; SN: 99002060159
Resource Relation:
Conference: 1997 workshop on the utilization of research reactors, Bandung (Indonesia), 6-13 Nov 1997; Other Information: PBD: Oct 1998; Related Information: Is Part Of Proceedings of the 1997 workshop on the utilization of research reactors; PB: 495 p.
Subject:
66 PHYSICS; PROTEINS; CRYSTALLOGRAPHY; NEUTRON DIFFRACTION; MONOCHROMATORS; HYDROGEN; LYSOZYME; LAUE METHOD; CRYSTAL STRUCTURE
OSTI ID:
327261
Research Organizations:
Japan Atomic Energy Research Inst., Tokyo (Japan)
Country of Origin:
Japan
Language:
English
Other Identifying Numbers:
Other: ON: DE99723943; TRN: JP9902207
Availability:
OSTI as DE99723943
Submitting Site:
JPN
Size:
pp. 173-178
Announcement Date:

Citation Formats

Niimura, Nobuo. Neutron protein crystallography. Japan: N. p., 1998. Web.
Niimura, Nobuo. Neutron protein crystallography. Japan.
Niimura, Nobuo. 1998. "Neutron protein crystallography." Japan.
@misc{etde_327261,
title = {Neutron protein crystallography}
author = {Niimura, Nobuo}
abstractNote = {X-ray diffraction of single crystal has enriched the knowledge of various biological molecules such as proteins, DNA, t-RNA, viruses, etc. It is difficult to make structural analysis of hydrogen atoms in a protein using X-ray crystallography, whereas neutron diffraction seems usable to directly determine the location of those hydrogen atoms. Here, neutron diffraction method was applied to structural analysis of hen egg-white lysozyme. Since the crystal size of a protein to analyze is generally small (5 mm{sup 3} at most), the neutron beam at the sample position in monochromator system was set to less than 5 x 5 mm{sup 2} and beam divergence to 0.4 degree or less. Neutron imaging plate with {sup 6}Li or Gd mixed with photostimulated luminescence material was used and about 2500 Bragg reflections were recorded in one crystal setting. A total of 38278 reflections for 2.0 A resolution were collected in less than 10 days. Thus, stereo views of Trp-111 omit map around the indol ring of Trp-111 was presented and the three-dimensional arrangement of 696H and 264D atoms in the lysozyme molecules was determined using the omit map. (M.N.)}
place = {Japan}
year = {1998}
month = {Oct}
}