APA

Ramón-Maiques S., Marina A., Uriarte M., Fita I. & Rubio V. (20000710). The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. : Journal of molecular biology.

Chicago

Ramón-Maiques S, Marina A, Uriarte M, Fita I and Rubio V. 20000710. The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. : Journal of molecular biology.

Harvard

Ramón-Maiques S., Marina A., Uriarte M., Fita I. and Rubio V. (20000710). The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. : Journal of molecular biology.

MLA

Ramón-Maiques S, Marina A, Uriarte M, Fita I and Rubio V. The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. : Journal of molecular biology. 20000710.