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Classical approaches for measuring this parameter\n                  <jats:italic>in vitro<\/jats:italic>\n                  involve tedious T4 DNA ligase-mediated cyclization kinetics experiments performed for one DNA fragment length at a time to establish effective local end-end concentrations (\n                  <jats:italic>J<\/jats:italic>\n                  -factors). Protein-mediated DNA looping is a more relevant biological reaction. An efficient approach to determine length-dependent protein-mediated DNA\n                  <jats:italic>J<\/jats:italic>\n                  -\n                  <jats:italic>loop<\/jats:italic>\n                  values\n                  <jats:italic>in vitro<\/jats:italic>\n                  has been lacking. We describe LOOP-TAG, a massively-parallel method. We leverage intramolecular DNA looping and tagmentation catalyzed by Tn5 transposase (Tnp) tethered to the terminus of a \u223c1,000-bp bead-bound duplex DNA. We detected loops terminating with Tnp. Counts of the resulting DNA looping-dependent bead-bound tagmentation products from deep sequencing determine DNA loop length probabilities at single-base pair resolution for all bead-bound fragments. When normalized to DNA fragment length probabilities from tagmentation using known concentrations of free Tnp, length-dependent\n                  <jats:italic>J<\/jats:italic>\n                  -\n                  <jats:italic>loop<\/jats:italic>\n                  values are directly determined. We demonstrate LOOP-TAG for Tnp tethered in two ways and in the presence of DNA-kinking architectural DNA binding protein Nhp6A. Intermediate length\n                  <jats:italic>J-loop<\/jats:italic>\n                  values are consistent with expectations of wormlike chain theory after accounting for strong sequence-dependence of Tnp. DNA loops are shifted to smaller sizes in the presence of Nhp6A, as predicted. 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