The third edition includes three new chapters. Janet Newman has written on optimization of crystallization hits (Chapter 18) as a follow-up to her earlier chapter on screening (Chapter 15). Martin Caffrey describes state-of-the art methods for membrane protein crystallization (Chapter 19), and Soneya Majumdar the preparation and crystallization of macromolecular complexes (Chapter 20). The A-Z section is revised and expanded in this edition. It is a repository for short topics, 80% of them new for this edition. Finally, five “how to” protocols are included. The reader may also notice there are more color figures and images. Color is easier to include in e-books, so this third edition reflects that.
This edition, like the first two (published in 1999 and 2010), is intended to be a practical guide for the person in the wet lab. As editor, I aimed to provide an overview of topics, assure cohesion between the chapters and sections of the book, and to guide the reader to related topics in other chapters. Overlap of topics is intentional for the readers who are not reading the book cover to cover. Written by the best experts in protein crystallization from different countries.
Edited by Terese M. Bergfors, Dept. of Molecular Biology, Uppsala University, Sweden.
Editorial Review, August 15, 2021
Reviewer: Terese Bergfors
Why are specialized texts on crystallization like this one necessary? In my job running a crystallization platform at Uppsala University, users ask many of the same questions in 2021 as they did when I started 37 years ago. But where can people find the answers? Details critical to the success of a crystallization experiment are rarely included in the published paper about the structure. Journals try to limit experimental detail to a minimum, or relegate it to supplementary materials. Even less is written about pitfalls to avoid. Books on crystallography usually only devote a single chapter to crystallization, given how much other material they must cover. Therefore a book like this one—devoted solely to crystallization—fills this gap of knowledge and skills.
But macromolecular crystallography faces challenges. As many as 70% to 80% of soluble proteins do not crystallize, and the odds are even worse still for membrane proteins. Will crystallization even still be necessary in the future? Will cryo-EM—which does not require crystals—end up replacing X-ray crystallography? My take on this is that the two techniques complement each other. If cryo-EM becomes the dominant method for elucidating structures, there will still be projects for which X-ray crystallography is better suited. The structural biologist would then need a source for information on how to crystallize—all the more so if the planetary pool of specialists in protein crystallization shrinks. The aim of this book is to be that information source.
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