Objections to the use of historical case studies for philosophical ends fall into two categories. Methodological objections claim that historical accounts and their uses by philosophers are subject to various biases. We argue that these challenges are not special; they also apply to other epistemic practices. Metaphysical objections, on the other hand, claim that historical case studies are intrinsically unsuited to serve as evidence for philosophical claims, even when carefully constructed and used, and so constitute a distinct class of challenge. We show that attention to what makes for a canonical case can address these problems. A case study is canonical with respect to a particular philosophical aim when the features relevant to that aim provide a reasonably complete causal account of the results of the historical process under investigation. We show how to establish canonicity by evaluating relevant contingencies using two prominent examples from the history of science: Eddington's confirmation of Einstein's theory of general relativity using his data from the 1919 eclipse and Watson and Crick's determination of the structure of DNA.

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The structures of protein and DNA were discovered primarily by means of synthesizing component-level information about bond types, lengths, and angles, rather than analyzing X-ray diffraction photographs of these molecules. In this paper, I consider the synthetic and analytic approaches to exemplify alternative heuristics for approaching mid-twentieth-century macromolecular structure determination. I argue that the former was, all else being equal, likeliest to generate the correct structure in the shortest period of time. I begin by characterizing problem solving in these cases as proceeding via the elimination of candidate structures through the successive application of component-level information and interpretations of X-ray diffraction photographs, each of which serves as a kind of constraint on structure. Then, I argue that although each kind of constraint enables the elimination of a considerable proportion of candidate structures, component-level constraints are significantly more likely to do so correctly. Thus, considering them before X-ray diffraction photographs is a better heuristic than one that reverses this order. Because the synthetic approach that resulted in the determination of the protein and DNA structures exemplifies such a heuristic, its use can help account for these discoveries.

Mitchell & Gronenborn (2017) propose that we account for the presence of multiple models of protein structure, each produced in different contexts, through the framework of integrative pluralism. I argue that two interpretations of this framework are available, neither of which captures the relationship between a model and the protein structure it represents or between multiple models of protein structure. Further, it inclines us toward concluding prematurely that models of protein structure are right in their contexts and makes extrapolation of findings from one context to another seem unwarranted. Instead, protein structure determination ought to be understood as modestly monistic. There is one model for every protein in each physicochemical context, and models of the same protein produced in different contexts are compatible with one another. 'Integrating' multiple models amounts to extrapolating from one context to another; this is possible because the effect of context on protein folding is relatively weak and predictable. Modest monism better describes the practice of protein structure determination than integrative pluralism and enables greater attention to how context affects protein folding.1 For instance, there might be 3 100 possible states for a polypeptide chain of just 100 amino acids, and this is on the conservative assumption that each amino acid can adopt only three conformations (Levinthal,