An attainable structural resolution of single particle imaging is determined by the characteristics of X-ray diffraction intensity, which depend on the incident X-ray intensity density and molecule size. To estimate the attainable structural resolution even for molecules whose coordinates are unknown, this research aimed to clarify how these characteristics of X-ray diffraction intensity are determined from the structure of a molecule. The functional characteristics of X-ray diffraction intensity of a single biomolecule were theoretically and computationally evaluated. The wavenumber dependence of the average diffraction intensity on a sphere of constant wavenumber was observable by small-angle X-ray solution scattering. An excellent approximation was obtained, in which this quantity was expressed by an integral transform of the product of the external molecular shape and a universal function related to its atom packing. A standard model protein was defined by an analytical form of the first factor characterized by molecular volume and length. It estimated the numerically determined wavenumber dependence with a worst-case error of approximately a factor of five. The distribution of the diffraction intensity on a sphere of constant wavenumber was also examined. Finally, the correlation of diffraction intensities in the wavenumber space was assessed. This analysis enabled the estimation of an attainable structural resolution as a function of the incident X-ray intensity density and the volume and length of a target molecule, even in the absence of molecular coordinates.