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Crambin
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| Crambin | |||||||
|---|---|---|---|---|---|---|---|
 Crystal structure of Crambin from PDB 3NIR [1] | |||||||
| Identifiers | |||||||
| Organism | |||||||
| Symbol | THI2 | ||||||
| UniProt | P01542 | ||||||
| |||||||
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]
References
[edit]- ^ Schmidt A, Teeter M, Weckert E, Lamzin VS (April 2011). "Crystal structure of small protein crambin at 0.48 Å resolution". Acta Crystallographica Section F. 67 (Pt 4): 424–8. doi:10.1107/S1744309110052607. PMC 3080141. PMID 21505232.
- ^ PDB: 3U7T; Chen JC, Fisher Z, Kovalevsky AY, Mustyakimov M, Hanson BL, Zhurov VV, Langan P (February 2012). "Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin". Acta Crystallographica Section F. 68 (Pt 2): 119–23. doi:10.1107/S1744309111051499. PMC 3274385. PMID 22297981.