S2
Protein S2 has an alpha-hairpin located within it. This was determined during the crystallization of the 30S subunit. The S2 protein is beloved to be involved in the mediation of interaction between the head of the ribosome and the protein (Wimberly et al 2000).

S3
The exact structure of protein S3 is not yet known. From the crystallization of 30S subunit, it was found that there is a beta-pleated sheet, along which alpha helices are stacked. There are two globular domains, alpha and beta. One of the domains is isolated from the RNA. Protein S3 is involved in a cluster with proteins S10 and S14. Hydrophobic interactions stabilize the cluster, which then helps stabilize the structure of the ribosome (Wimberly et al 2000).

S10
It has been found through crystallization of the 30S subunits that S10 contains alpha helices packed against a beta-pleated sheet. It also contains either a long hairpin or loop, which either could be used to interact with 16S rRNA. Protein S10 is involved in a cluster with proteins S3 and S14. Hydrophobic interactions stabilize the cluster, which then helps stabilize the structure of the ribosome (Wimberly et al 2000).

S11
S11 has a beta sheet with alpha helices stacked around it. The Beta sheet is located near the minor groove of 16S rRNA. S11 is packed flatly against the groove. Also, S8 has an extended tail from either the carboxyl or amino end of the protein. The extension allows the protein to interact with 16S rRNA and make contact with the rRNA (Wimberly et al 2000).