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I .The purification and crystallization of 2-phospho-~-glycerate hydro-lyase from human skeletal muscle is described.2 . Preparations of the crystalline enzyme were found to be homogenous as examined in free boundary and gel electrophoresis. Chromatography on Sephadex G 75 and TEAE-cellulose revealed only one component.3. The sedimentation constant was found to be 5.9 x see, the diffusion constant 5.6 x 10-7 cmZ/sec and the intrinsic viscosity 4.10 ml/g. The molecular weight calculated from these data was found to be 95,000 f 3,000, and the frictional ratio 1.26. 4. The properties of the enzyme are compared with those of phosphopyruvate hydratase from rabbit muscle and yeast.

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