Φορτώνει......
Crystallization and preliminary X-ray analysis of hyperthermophilic l-threonine dehydrogenase from the archaeon Pyrococcus horikoshii
Recombinant l-threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii was prepared using an Escherichia coli expression system. The hyperthermostable l-threonine dehydrogenase consists of 348 amino acids with a molecular weight of 37.7 kDa. The enzyme was crystallized by th...
Αποθηκεύτηκε σε:
| Κύριοι συγγραφείς: | , , , |
|---|---|
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
International Union of Crystallography
2005
|
| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1952418/ https://ncbi.nlm.nih.gov/pubmed/16511061 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S174430910500881X |
| Ετικέτες: |
Προσθήκη ετικέτας
Δεν υπάρχουν, Καταχωρήστε ετικέτα πρώτοι!
|