Several protein ensembles facilitate meiotic crossover recombination and the associated process of synaptonemal complex (SC) assembly during meiosis. We have employed proximity labeling as a phenotyping tool to investigate functional requirements for spatial relationships between meiotic recombination and SC proteins in S. cerevisiae, and to gain deeper insight into the molecular deficits of crossover-deficient meiotic mutants. We find that recombination initiation and synaptonemal complex structures are dispensable for proximity labeling of the Zip3 E3 ligase by components of the ZZS ensemble (Zip2, Zip4 and Spo16) but enzymes associated with early steps in recombination are required for Zip3 proximity labeling by MutSg, consistent with the possibility that MutSg joins Zip3 only after a specific recombination intermediate has been generated. Proximity labeling furthermore suggests that a key defect of crossover-defective, SC-proficient zip1 separation-of-function mutants is a failure to assemble an early recombination ensemble where MutSg can properly engage Zip3. We also find that the SC structural protein Ecm11 is proximity labeled by ZZS proteins in a Zip4-dependent and Zip1-independent manner, but by Zip3 and Msh4 at least in part via a distinct pathway that relies on Zip1. Finally, streptavidin pulldown followed by mass spectrometry on eleven proximity labeling strains uncovered shared proximity targets of SC and crossover-associated proteins, some of which have not yet been implicated in meiotic recombination or SC formation highlighting the potential of proximity labeling as a discovery tool.