[en] Single biomolecular imaging using XFEL radiation is an emerging method for protein structure determination using the ''diffraction before destruction'' method at near atomic resolution. Crucial parameters for such bio-imaging experiments are photon energy range, peak power, pulse duration, and transverse coherence. The largest diffraction signals are achieved at the longest wavelength that supports a given resolution, which should be better than 0.3 nm. We propose a configuration which combines self-seeding and undulator tapering techniques with the emittance-spoiler method in order to increase the XFEL output peak power and to shorten the pulse duration up to a level sufficient for performing bio-imaging of single protein molecules at the optimal photon energy range, i.e. around 4 keV. Experiments at the LCLS confirmed the feasibility of these three new techniques. Based on start-to-end simulations we demonstrate that self-seeding, combined with undulator tapering, allows one to achieve up to a 100-fold increase in peak-power. A slotted foil in the last bunch compressor is added for X-ray pulse duration control. Simulations indicate that one can achieve diffraction to the desired resolution with 50 mJ (corresponding to 10¹⁴ photons) per 10 fs pulse at 3.5 keV photon energy in a 100 nm focus. This result is exemplified using the photosystem I membrane protein as a case study.