Ribulose-1,5-bisphosphate carboxylase/oxygenase is the key enzyme for photosynthesis. The wild-type and mutant (aminoacid substitutions in the catalytically important loop 6 region) enzymes from Chlamydomonas reinhardtii, a unicellular green alga, were crystallized. Wild-type, single-mutant (V331A) and two double-mutant (V331A/T342I and V331A/G344S) proteins were activated with cofactors CO 2 and Mg 2+ , complexed with the substrate analog 2 H -carboxyarabinitol-1,5-bisphosphate, and crystallized in apparently isomorphous forms. Unit-cell determinations have been completed for three of the enzymes.
vapor diffusion method at 20•C. The crystals of azmin-I belong to the monoclinic crystal system and have space group C2 with unit cell parameters of a=l30.6A, b=54.4A, c=74.7 A, and b=96.l•. Four molecules are in the asymmetric unit. The crystals of azmin-II belong to the tetragonal crystal system and have space group ?4122 ,,;th unit cell p';rameters a=b=52.6A, c=100.7 A. Only one molecule is in the asymmet1ic unit. They diffract up to 2.8A and 2.0A resolutions, respectively. Their crystal structures were solved by molecular replacement method using AMoRe in the CCP4. Molecular structure of Azurin ll from Alcaligenes Xylosoxidans NCIB 11015 was chosen as a starting model for both azurins. The refinement for both azmins is being carried out by XPLOR.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.