Filia is one of the components of maternal Subcortical Maternal Complex(SCMC). The N-terminal of Filia is similar to KH domain of type I family, which play roles in transcription regulation in oogenesis and embryo development by binding RNA. Additionally, maternal Filia plays essential role in maintaining euploidy. The absence of maternal Filia appears to delay embryonic progression, which can decrease the number of offspring rather than sterile. During oocyte maturation stage, the concentration of GSH varied to keep balance of oxidation-reduction. Our crystallographic studies successfully reveal the structure of Filia N-terminal protein grown in solution with GSH. In contrast with the structure of Filia N-terminal protein grown in condition free of GSH, protein grown in GSH have five pairs of dimer in an asymmetry unit. Domain swapping occurs in the α3-helix of Filia (N1-124) molecules. A special decamer structure is formed by ionic interaction, H-bond and hydrophobic interaction. The Filia N-terminal structure provides a structural foundation for further researches on the structure and function of Filia in diversity physiological environment.