The crystallization experiments of 14 proteins were carried out, the experiment was lasted 16.5 days by using German Biobox facility and self-developed growth chambers aboard Shenzhou-8 spaceship. The counterpart experiment was performed on the ground laboratory according to the same timing sequence. The results show that 12 of 14 proteins precipitate crystals in space experiment, 11 of 14 proteins precipitate crystals on ground experiment. Eight space-grown crystals of four proteins are applied to synchrotron radiation, and eight set diffraction data are obtained. In the meantime, five earth-grown crystals of three proteins are applied to synchrotron radiation, and five set diffraction data are obtained, among them, one set is incomplete. The highest preliminary diffraction resolutions of space- and earth-grown lysozyme crystals are 1.16Å and 1.23Å, respectively. However, is the highest resolutions are 1.75Å and 1.49Å, respectively for the crystals of diadenosine tetraphosphate from dysentery bacillus; nevertheless one space-grown crystal has different crystallographic symmetry from other crystals. The highest diffraction resolution for the space-grown crystal of the chlamydial protease-like activating factor diffracted is 2.31Å, the ground one fails to diffraction. The highest diffraction resolution for the space-grown crystal of 17β-hydroxysteroid dehydrogenase type 7 complex from Canada is 2.30Å, the ground one is not good enough for collecting a complete diffraction data set. The growth chambers used in space experiment adopt a new structure for the first time in the world of which the protein solution container is made of glass capillary and immersed in the precipitation solution. The new growth chamber is portable, works without power supply, and is able to eliminate Marangoni convection in the vapor diffusion chamber.