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Book Review Methods in Enzymology. Vol. 114 and 115. Diffraction Methods for Biological Macromolecules Edited by H. W. Wyckoff C. H. W. Hirs and S. N

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BOOK R E V I E W S
Methods in Enzymology. Vol. 114 and 115. Edited by H. W .
Wyckofl, C. H. W . Hirs, and S . N. Timashefl. Academic
Press, New York 1985. Vol. 114: Diffraction Methods for
Biological Macromolecules, Part A, xxiv, 588 pp., hardcover, $ 64.00;-1SBN 0-12-182014-9. Vol. 115: Part B,
xxii, 485 pp., hardcover, $ 55.00;-ISBN 0-12-182015-7
Despite the impressive developments in N M R spectroscopy in recent years, which now allow the secondary and
tertiary structures of small polypeptides (< 10000 daltons)
to be determined in solution, X-ray crystallography will
probably remain the only method capable of providing detailed structural information (namely, three-dimensional
atomic coordinates) on larger, globular proteins. Whereas
application of N M R techniques to the determination of
protein structure is limited by the requirements that the
protein be available in large amounts, be sufficiently soluble, and exhibit good stability, the use of protein crystallography primarily depends on the ability to crystallize the
macromolecule. Once suitable crystals of the protein have
been obtained, the elucidation of its structure can be accomplished within a reasonable length of time, provided
that its amino acid sequence is known.
New techniques for the collection of diffraction data
(area detectors) and for the interpretation of electron density (high-resolution vector graphics) have not only decreased the time required for protein structure determination, but, even more importantly, have improved the accuracy of the structures obtained. Crystallographic refinement has progressed to a point where the methods available, while still requiring considerable patience, often afford. atomic coordinates with error limits of only 0.1 to
0.2 A. Such highly refined protein structures are, in turn,
essential for modeling the interaction of these proteins
with small molecules, such as substrates and inhibitors, o r
for planning site-directed mutagenesis experiments. These
applications, in particular, have made protein crystallography an interesting and potentially important tool for the
pharmaceutical industry.
The rapid development of this field makes periodic reviews of protein crystallographic methods all the more urgent, but these have been lacking so far. The standard textbook on protein crystallography by Blundell and Johnson
is now ten years old and therefore no longer u p to date,
although it remains an essential source of information.
Thus, there has been a crucial need for a current description of the new methods of high-resolution protein crystallography. This gap has now been filled by Volumes 114
and 115 of the renowned series “Methods in Enzymology.”
Well-known experts have contributed a total of 63 articles,
which provide a more or less comprehensive account of
protein crystallography. The individual contributions have
been organized into sections dealing with the historical development of the field, crystallization, data collection,
phase determination, model building, and presentation of
the results. This arrangement, however, is not always optimal. For example, the clearly written article by R. Sparks
on least-squares refinement is included, less than ideally,
in the chapter on phase determination.
The volumes are a gold mine for the specialist if only
because of the nearly 700 references to the scientific literature, which cover developments u p to 1982 and even include articles published in 1984. It is questionable, howevAngew. Chem. In!. Ed. Engl. 26 (1987) No. 4
er, whether the volumes achieve the goal explicitly stated
in the introduction, namely, to provide biochemists with
a n introduction to macromolecular diffraction methods.
This goal is a priori unrealistic for a work consisting of
differently arranged contributions from a number of individuals. An exception is the collection of well-written articles on the crystallization of biological macromolecules,
which should provide many biochemists with useful insights.
Some of the contributions are more technical in nature
o r describe specific computer programs; others are comparable to well-planned review articles. Even unpublished
material is to be found: The method of “iterative single
isomorphous replacement” of B. C. Wang, which is best
described by the term “electron density modification” (although the author specifically disapproves of this term-]
trust he will forgive me), is described here in detail for the
first time. This method has been used for the past three
years by many protein crystallographers with considerable
success-an indication of the excellent communication
within this scientific community.
Only a few topics are not covered by these volumes. For
example, the important technique of phase combination is
not mentioned at all. On the other hand, the section on the
systematics of protein structures is remarkably encompassing (with very instructive pictures by Jane Richardson, Arthur Lesk, and Karl Hardman!). For this reason, Volume
115, in particular, is recommended to all those interested
in protein structures, namely, spectroscopists, gene technologists, and theoreticians. Both volumes, however, belong on the book shelf of every protein crystallographer.
Rolf Hilgenfeld [NB 796 IE]
Hoechst AG, Frankfurt am Main (FRG)
Regulation of Secondary Metabolite Formation. Proceedings of the Sixteenth Workshop Conference, Hoechst,
Gracht Castle, 12-16 May 1985. Edited by H . Kleinkauf.
H. von Dohren, H . Dornauer, and G . Nesemann. VCH
Verlagsgesellschaft, Weinheim 1986. xx, 402 pp., bound,
D M 108.00.-ISBN 3-527-26475-2
The production of antibiotics using microorganisms is one
of the standard tasks of biotechnology. Mutation and selection have been used to obtain strains giving the best
production. This empirical procedure has been employed
without knowing how the formation of secondary metabolites depends on the regulating processes. It is remarkable
that, in spite of the great importance of antibiotics, the genetic instability of high performance strains is not yet understood, nor has an adequate bridge been established between our knowledge of the biosynthesis of antibiotics and
that of the genetics of the organisms which produce them.
The mutagenic mechanism for even such a technologically
important group as the Streptomycetes is much less well
understood than that for the classical model Escherichia
coli.
It therefore seems very appropriate that the 16th Workshop conference arranged by Farbwerke Hoechst was on
microbiology, being concerned with the topical theme of
secondary metabolites. Twenty papers by acknowledged
experts from throughout the world were presented.
367
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