Crystal structure of Crambin from PDB 3NIR 
Crambin is a small seed storage protein from the Abyssinian cabbage. It belongs to thionins. It has 46 residues (amino acids). It has been extensively studied by X-ray crystallography since its crystals are unique and diffract to a resolution of 0.48 Å. Neutron scattering measurements are available also at a resolution of 1.1 Å, PDB ID 3U7T.
- Andrea Schmidt; Martha Teeter; Edgar Weckert; Victor S. Lamzin (May 2011). "Crystal structure of small protein crambin at 0.48 Å resolution". Acta Crystallographica Section F. 67 (4): 424–428. doi:10.1107/S1744309110052607. PMID 21505232.
- J. C.-H. Chen; Z. Fisher; A. Y. Kovalevsky; M. Mustyakimov; B. L. Hanson; V. V. Zhurov; P. Langan (2012). "Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin". Acta Crystallographica Section F. 68 (2): 119–123. doi:10.1107/S1744309111051499.