Crambin
| Crambin | |
|---|---|
 Crystal structure of Crambin from PDB 3NIR [1] | |
| Identifiers |
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,[2] PDB ID 3U7T.
References
- ↑ Andrea Schmidt, Martha Teeter, Edgar Weckert, Victor S. Lamzin (May 2011). "Crystal structure of small protein crambin at 0.48 Å resolution". Acta Crystallogr Sect F Struct Biol Cryst Commun. 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 and 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: 119–123. doi:10.1107/S1744309111051499.