While interpreting mass spectra can be a daunting task, Smith offers a very important reminder that significant structural information can be gleaned from even the most difficult mass spectrum and that by following a few basic steps and being persistent, one might be able to determine structures of unknowns. However, attempting to interpret mass spectra of poor quality is definitely not worthwhile, so the author presents a brief and informative set of criteria for judging the quality of a mass spectrum. These criteria include the presence of isotope peaks and a good signal-to-background ratio free of spurious peaks arising from contaminants or GC column bleed. He cautions that these criteria should be carefully considered even when comparing an apparent match between an unknown mass spectrum with that from a standard reference library.

Relevant and useful introductory chapters provide very brief descriptions of ionization methods including EI, chemical ionization (CI), electrospray ionization (ESI), and matrix-assisted laser desorption/ionization (MALDI). Surprisingly, fast atom bombardment (FAB) receives very little mention despite its success in generating useful mass spectra for small, polar compounds, and no sample mass spectra are shown for FAB, ESI, or MALDI. Likewise, the section on mass analyzers describes time-of-flight, magnetic sector, transmission quadrupole, and quadrupole ion trap but omits the fourier transform ion cyclotron resonance mass spectrometer. Unfortunately, the only tandem MS instrument described in any detail is the triple quadrupole configuration and only the product ion experiment is mentioned. Indeed, the use of these “soft” ionization methods coupled with either tandem MS or multiple stages of MS (MSⁿ) for mapping post-translational modifications in proteins represents an example of state-of-the-art structure elucidation via MS.

This book contained a few pleasant surprises along the way. These include the description of classic deuterium labeling studies of 2-pentanone that helped elucidate the mechanisms of the McLafferty rearrangement and the work of Beynon and others to elucidate the ortho substituent effect. Generous use of citations will help those wishing to find more in-depth discussions or descriptions of particular topics. Detailed fragmentation mechanisms are clearly drawn, ample figures and tables properly supplement the body of the text, and carefully chosen practice problems reinforce the important concepts presented in each chapter.

What most distinguishes this book from others on the topic is the offering of and the emphasis on an overall strategy for spectral interpretation. Rather than simply catalogue fragmentations and rearrangements of various compound classes, the author provides a set of guidelines to follow for successful spectral interpretation. Drawing on his background in forensic science, Smith chooses examples of illicit drugs of abuse such as valium, cocaine, and Δ⁹ –tetrahydrocannabinol (THC) to illustrate his points. The interpretation of these rather difficult mass spectra may overwhelm the least committed student, but the author deserves much credit for his exhaustive explanations in these examples.

While providing a rational strategy for EI mass spectral interpretation, Smith manages to establish realistic expectations for users of MS data that, in turn, should foster better appreciation for the capabilities and limitations of MS. Perhaps future editions of this text will expand upon many more of the capabilities of MS, including the coupling with liquid chromatography, the utility of MS² and MSⁿ experiments, and the promise of the field of proteomics to provide important insights into molecular level structure/function relationships in complex biological pathways.