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Protease inhibitors play key roles in physiological processes. Arrowhead protease inhibitor A (API-A), a member of the serine protease inhibitor family, can inhibit two trypsin molecules simultaneously. In the present work, API-A from Sagittaria sagittifolia has been cloned, expressed, purified and crystallized in complex with bovine trypsin. The crystals were obtained by the sitting-drop method. A data set was collected to 2.48 Å resolution from a single crystal. The crystal belonged to space group C2221, with unit-cell parameters a = 76.63, b = 110.86, c = 152.99 Å, α = β = γ = 90°.

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