Growing protein crystals that are sufficiently large and of sufficient quality for conventional x-ray structure analysis can be extremely challenging. Many biologically significant proteins including most membrane proteins tend to form disordered crystals which diffract poorly or whose diffraction is contaminated by the presence of defects. Under the assumption of perfect crystallinity protein structure determination from these types of samples is challenging and the reliability and quality of the structures thus obtained can be significantly degraded.
In a 2013 paper by Dilanian et al.  our group demonstrated that inclusion of oversampled Bragg Coherent Diffractive Imaging (BCDI) data could improve the quality of protein structure recovered from disordered nanocrystals at an X-ray Free Electron Laser (XFEL). The current work aims to extend these ideas to synchrotron based protein crystallography from disordered micron-sized crystals in cases where structure retrieval using conventional crystallographic approaches has failed. Here I will discuss the basic theory underpinning these ideas as well as present the first experimental BCDI data collected from micron-sized protein crystals of Lysozyme.
 R. Dilanian, V. Streltsov, H. M. Quiney, and K. Nugent, “Continuous X-ray diffractive field in protein nanocrystallography.,” Acta crystallographica. Section A, Foundations of crystallography, vol. 69, no. Pt 1, pp. 108–18, Jan. 2013.