The problem of pentamer packing on a two-dimensional plane is of concern not only in physics and mathematics but also in biology. The packing styles of pentamers may either be related to or reflect the physiological or biochemical properties of biological macromolecules. C-reactive protein (CRP), one of the classical members of the petraxin family, was recently two-dimensionally (2D) crystallized by us on lipid monolayers by specific adsorption (Wang, H. W., and Sui, S. F., 1999, J. Struct. Biol. 127, 283-286). Another type of the protein's 2D crystal under the same conditions was obtained in the present work. The new 2D crystal was studied using electron microscopy of negatively stained specimens followed by image processing. A projection map at 2.2-nm resolution was obtained. The previous 2D crystal (PI) and the current 2D crystal (PII) show different pentamer-packing styles. Both of them are closely related to the fivefold symmetry of the molecule itself. The coexistence and the spatial contiguity of the two types of pentamer assembly were observed in a visual field. The fivefold symmetrical macromolecule can form a pentiling pattern on a two-dimensional plane, which has never been reported in biological system before. The possible mechanism of the two-dimensional assembly of pentameric CRP on lipid monolayers is discussed.