26:
126:(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.
204:"Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin"
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202:
Chen JC, Fisher Z, Kovalevsky AY, Mustyakimov M, Hanson BL, Zhurov VV, Langan P (February 2012).
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145:"Crystal structure of small protein crambin at 0.48 Å resolution"
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25:
142:
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Schmidt A, Teeter M, Weckert E, Lamzin VS (April 2011).
249:
30:Crystal structure of Crambin from PDB 3NIR
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168:
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208:Acta Crystallographica Section F
149:Acta Crystallographica Section F
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1:
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7:
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220:10.1107/S1744309111051499
161:10.1107/S1744309110052607
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114:from the Abyssinian
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214:(Pt 2): 119–23.
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118:. It belongs to
110:is a small seed
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73:
48:
46:Crambe hispanica
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155:(Pt 4): 424–8.
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112:storage protein
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122:. It has 46
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86:Swiss-model
36:Identifiers
130:References
82:Structures
77:Search for
200:;
258:Proteins
252:Category
238:22297981
179:21505232
124:residues
120:thionins
96:InterPro
41:Organism
229:3274385
170:3080141
116:cabbage
108:Crambin
92:Domains
62:UniProt
19:Crambin
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167:
67:P01542
53:Symbol
234:PMID
197:3U7T
175:PMID
56:THI2
224:PMC
216:doi
193:PDB
165:PMC
157:doi
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212:68
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159::
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