The transition-state complex of this 42 kDa homologue of creatine kinase has been refined at 1.2 Å resolution. It indicates that precise positioning of substrates and restriction of the active-site motion are important components in catalysis.
|Original language||English (US)|
|Number of pages||9|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - Dec 1 2002|
ASJC Scopus subject areas
- Structural Biology