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Human salivary cystatin, a thiol proteinase inhibitor, has been implicated in potential antimicrobial and antiviral functions of saliva. A variant of human salivary cystatin SN expressed and purified in an Escherichia coli expression system lacking residues 12–16 near the N-terminus (Δ12–16) has been crystallized by the vapor-diffusion technique. The crystals are of the hexagonal space group P622 and have cell constants of a = 85.41, b = 85.41, c = 131.6 Å, α = β = 90, γ = 120°, and contain two molecules of molecular weight 13 500 per asymmetric unit. The crystals diffract up to a resolution of 2.2 Å and are suitable for X-ray diffraction analysis.

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