The folding process of a single chain including coil-globule transition and crystallization has been investigated through dynamic Monte Carlo simulations. The results based upon ensemble averaging illustrated three distinct states: coil, molten globule, and globule states. Furthermore, the crystallization process from these collapsed states demonstrated various characteristics and it also verified the thermodynamic partitions. The isothermal crystallization in the three states showed the folding rates, and the final crystallite morphologies strongly depended on the collapsed states. Especially, the onset temperature of crystallization in the intermediate molten globule state demonstrated the strongest sensitivity to the solvent qualities in the three different states. Moreover, the crystallization in this intermediate state illustrated a two-step folding mechanism with the prior dense core serving as a precursor to induce the subsequent crystallization. Our observations would help in understanding the thermodynamics and kinetics of phase transition of a single macromolecule. Possible relations to the protein folding were also discussed.