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Literature summary extracted from
- Cloning, expression, purification, crystallization and initial crystallographic analysis of the preprotein translocation ATPase SecA from Thermus thermophilus (2006), Acta Crystallogr. Sect. F, F62, 909-912.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.4.2.5 | - |
Thermus thermophilus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 7.4.2.5 | crystallization by hanging-drop vapour-diffusion technique in two different space groups P2(1(2))21 (a = b = 168.6 A, c = 149.8 A) and P6(1(5))22 (a = b = 130.9 A, c = 564.6 A). The crystals, improved by macroseeding, diffract to beyond 2.8 A and 3.5 A resolution for the trigonal and hexagonal crystal forms, respectively | Thermus thermophilus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.4.2.5 | Thermus thermophilus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.4.2.5 | - |
Thermus thermophilus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.4.2.5 | preprotein translocation ATPase SecA | - |
Thermus thermophilus |
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