A small DNA-binding protein (Ssh10b) from the hyperthermophilic archaeon Sulfolobus shibatae was crystallized. The crystals could only diffract to 0.65 nm. And gel medium was used to improve the diffraction resolution. Gel adding led to slower speed of crystallization, change of crystal morphology and shortening of C axis of unit cell. The crystals grown in gel medium could diffract to 0.35 nm, and a set of data was collected.