Objective：To determine the three dimensional structure and to analyze the molecular mechanism of staphylococcus aureus（S.aureus） infection for developing a new antibacterial drugs by cloning，expressing，purifying and crystallizing the surface protein SdrE from S.aureus. Methods：SdrE gene was amplified and cloned into the vector. Recombinant plasmid，pW28-SdrE，was trans－formed into E.coli B834 to express SdrE protein. SdrE protein was purified by Ni2+-NTA affinity chromatography column and DEAE anion-exchange chromatography column. State of aggregation in solution was analyzed by Hiload Superdex 200 gel flittration column. SdrE crystal was screened with Hampton kit and crystal was optimized with chessboard method. Results：（1）Recombinant plasmid pW28-SdrE was constructed and expressed in soluble form in E.coli B834 strain. （2）Puried SdrE exhibited as monomer in solution. （3）Single crystals of SdrE with good shape and diffraction capability were obtained. Conclusions：SdrE crystals can be grown by classic protein purification and crystal cultivation methods，which provides an important base for structural and functional study of SdrE in future and is necessary for developing new antibacterial drugs.