Table Of ContentNeutrons
in Biology
BASIC LIFE SCIENCES
Alexander Hollaender, General Editor
Associated Universities, Inc., Washington, D.C.
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Neutrons
in Biology
Edited by
Benno P. Schoenborn
Brookhaven National Laboratory
Associated Universities, Inc.
Upton, New York
Springer Science+Business Media, LLC
Library of Congress Cataloging in Publication Data
Main entry under title:
Neutrons in biology.
(Basic life sciences; v. 27)
"Proceedings of the 32nd Brookhaven symposium in biology, held June 1-4, 1982,
at Brookhaven National Laboratory, Upton, New York"—T.p. veerso.
Includes bibliographical references and index.
1. Neutrons—Scattering—Congresses. 2. Biology—Methodology—Congresses. I.
Schoenborn, Benno P. II. Brookhaven National Laboratory. III. Series.
QH324.9.N48N48 1984 574.8/8/028 83-24708
ISBN 978-1-4899-0377-8 ISBN 978-1-4899-0375-4 (eBook)
DOI 10.1007/978-1-4899-0375-4
Proceedings of the 32nd Brookhaven Symposium in Biology, held June 1-4, 1982,
at Brookhaven National Laboratory, Upton, New York
© Springer Science+Business Media New York 1984
Originally published by Plenum Press, New York in 1984
Softcover reprint of the hardcover 1st edition 1984
All rights reserved
No part of this book may be reproduced, stored in a retrieval system, or transmitted,
in any form or by any means, electronic, mechanical, photocopying, microfilming,
recording, or otherwise, without written permission from the Publisher
PREFACE AND ACKNOWLEDGEMENTS
This second symposium on the use of neutron scattering
analysis of biological structures is dedicated to the memory of
Sir James Chadwick, who discovered the neutron just 50 years
ago. The first symposium covering this new application of neutron
physics was held here at Brookhaven National Laboratory seven
years ago and was characterized by a lot of enthusiasm and
expectation. Now, seven years later, the field has matured, and
some of the expectations, particularly in small-angle scattering,
have been fulfilled, while expectations on dynamic studies have
not. The prospects of future advances in dynamic study are,
however, high, and observations on polymers suggest that present
instruments do have adequate resolving power for the study of bio
polymers. Many of the advances presented in this volume rest on
isotopic substitution studies and efficient position-sensitive
detectors, developments that were highlighted in the last
symposium and that were perfected during the last seven years.
The Committee wishes to thank the speakers and chairmen for
their participation. The Committee also wishes to express
appreciation to the Dr. Alexander Hollaender Fund and the U. S.
Department of Energy for support of this meeting.
We thank the referees who reviewed the papers, and we
particularly wish to thank Margaret Dienes, Helen Z. Kondratuk,
Kathryn Kissel, and Susan Lamm for preparing the papers for
printing.
This 32nd Brookhaven Symposium in Biology was held under the
auspices of the U. S. Department of Energy.
Symposium Committee
Benno P. Schoenborn, Chairman
R. Douglas Carlson
Anthony A. Kossiakoff
Anand M. Saxena
Dieter K. Schneider
v
CONTENTS
SESSION I
Plenary Lecture:
Comments on Some Present and Future Problems
in Protein Structure........................................ 1
F.M. Richards
SESSION II. Chair: D.E. Engelman
Structural Elements of the 50 S Subunit of
E. Coli Ribosomes •••••••••••••.••••••••••••••••••••••••••••• 25
- R.P. May, H.B. Stuhrmann, and K.H. Nierhaus
Neutron Scattering Studies of the H2a-H2b and
(H3-H4)2 Histone Complexes.................................. 47
R. D. Carlson
Symposium Lecture:
Neutron Scattering and the 30 S Ribosomal Subunit
of E. Co 11. • • • • • • • • • • • • • • • • • • • • • • • • . • • . • • • • • • • • • • • • • • • • • • • • • 73
P~B. Moore, D.M. Engelman, J.A. Langer,
V.R. Ramakrishnan, D.G. Schindler, B.P. Schoenborn,
I-Y. Sillers, and S. Yabuki
The Solution Structures of Transfer RNA and
Ribonuclease in Different Solvents •••••••••••••••••••••••••• 93
G. Zaccai
SESSION III. Chair: W.C. Koehler
The Crystal Structure of the Nucleosome Core Particle
by Contrast Variation ••••••••••••••••••••••••••••••••••••••• 105
G.A. Bentley, J.T. Finch, A. Lewit-Bentley, and M. Roth
A New Neutron Small-Angle Diffraction Instrument at the
Brookhaven High Flux Beam Reactor ••••••••••••••••••••••••••• 119
D.K. Schneider and B.P. Schoenborn
Neutron Optics with Multilayer Monochromators ••••••••••••••••• 143
A.M. Saxena and C.F. Majkrzak
vii
viii CONTENTS
SESSION IV. Chair: V. James and D.L.D. Caspar
Membranes and Cellular Biology: Questions of
Detail or Framework......................................... *
D. Worcester
Neutron Diffraction Studies on Incorporation of
Hexane into Oriented Lipid Bilayers ••••••••••••••••••••••••• 159
G.I. King, N.-M. Chao, and S.H. White
Symposium Lecture:
Neutron Scattering Studies of Virus Structure ••••••••••••••• 173
S. Cusack
Specific Deuteration and Membrane Structures •••••••••••••••••• 189
G. B6ldt
SESSION V. Chair: D. Worcester
Neutron Diffraction and the Decomposition of
Membrane Scattering Profiles into the Scattering
Profiles of Their Molecular Components •••••••••••••••••••••• 201
J.K. Blasie, J.M. Pachence, and L.G. Herbette
Structural Studies of Plasma Lipoproteins ••••••••••••••••••••• 211
D. Atkinson and G.G. Shipley
Neutron Diffraction Studies of Bacteriorhodopsin
Structure. • . . • . . . . . . . . . . • • • . . . • . • . • . . . . . . • . . . • • • • . . . • • . . . . .• 227
J. Trewhel1a, E. Gogol, G. Zaccai, and D.M. Engelman
SESSION VI. Chair: G. Kartha and P.B. Moore
The Structure of Bound Water and Refinement of
Acid Metmyoglobin ••••••••••••••••••••••••••••••••••••••••••• 247
N.V. Raghavan and B.P. Schoenborn
A Protein Structure is Only as Good as the Data ••••••••••••••• 261
B.P. Schoenborn
Symposium Lecture:
Use of the Neutron Diffraction--H/D Exchange Technique
to Determine the Conformational Dynamics of Trypsin ••••••••• 281
A.A. Kossiakoff
Hydrogen Bonding and Exchange in Oxymyoglobin ••••••••••••••••• 305
S.E.V. Phillips
*No manuscript submitted.
CONTENTS ix
SESSION VII. Chair: S.E.V. Phillips
Deuterium Exchange in Lysozyme at 1.4-i Resolution •••••••••••• 323
S.A. Mason, G.A. Bentley, and G.J. McIntyre
The Neutron Structure of the Hydrophobic Plant
Protein erambin •••••••••••••.•.••••.•••••••••••••••••••••••• 335
M.M. Teeter and A.A. Kossiakoff
Application of Joint Neutron and X-Ray Refinement to
the Investigation of the Structure of Ribonuclease A
at 2.0-1 Resolution •••••.•••••.••••....••.•••••••.•.•••••••• 349
A. Wlodawer and L. Sj8lin
SESSION VIII. Chair: B. Jacrot and G. Zaccai
Inelastic Neutron Scattering Studies of Hexokinase
in Solution •................................................ 365
D.M. Engelman, A.J. Dianoux, S. Cusack, and B. Jacrot
Neutron Spectroscopy of Hydrogenous and Biosynthetically
Deuterated Proteins ••••••••••••••••••••••••••••••••••••••••• 381
H.D. Middendorf, J.T. Randall, and H.L. Crespi
Inelastic Scattering From Biomolecules: Principles
and Prospects............................................... 401
H.D. Middendorf
Concluding Remarks •••••••••••••••••••••..••...•••••••••••••••• 437
P.B. Moore
ABSTRACTS OF POSTER PRESENTATIONS ••••••••••••••••••••••••••••• 441
PAR.TICIPAN'TS •••••••••••••••••••••••••••••••••••••••••••••••••• 453
INDEX. • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • •• 457
COMMENTS ON SOME PRESENT AND FUTURE PROBLEMS IN PROTEIN STRUCTURE
Frederic M. Richards
Department of Molecular Biophysics and Biochemistry
Yale University
New Haven, CT 06511
DIFFRACTION FROM CRYStALS
In 1964 some program officers at NIH were seriously, and
understandably, concerned that the solution of the myoglobin
structure might have been an accident. The intense effort that
had been going on in the field of protein crystallography during
the previous five years had not produced any additional structures
and perhaps would not in the foreseeable future. The dramatic
appearance of the lysozyme model in 1965 fortunately put an end to
thoughts of major funding shifts that were being discussed. Let
us hope some comparable event occurs this year.
Today, if a protein can be induced to crystallize, it can be
assumed with considerable confidence that the structure will come
along in due time, some, of course, more easily than others. The
tricks of the trade are being codified and constantly improved.
If permitted by the present Government, Brookhaven will have an
increasingly important role in the future in providing the possi
bility of very rapid data collection and reduction, allowing many
more individuals to work out their own structures without exten
sive structure laboratories of their own. One hopes the old hands
will still be needed to provide solace and advice on the inevi
table pitfalls that always arise. The quality of the structure
will depend only on the quality of the crystals. Quality in this
sense means the precision with which the mean atomic positions can
be specified.
It should be recognized that our most detailed knowledge of
protein structure is based on those systems which provide high
quali ty crys tals • This may be a very restricted, albeit con
stantly expanding, subset of all proteins, and our impressions of
protein structure may thus be biased to an extent at present
