Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-.ANG. resolution: identification of the active site and possible catalytic residues

MLA

George L. Kenyon, et al. “Mechanism of the Reaction Catalyzed by Mandelate Racemase. 2. Crystal Structure of Mandelate Racemase at 2.5-.ANG. Resolution: Identification of the Active Site and Possible Catalytic Residues.” Biochemistry, vol. 30, Sept. 1991, pp. 9264–73. EBSCOhost, https://doi.org/10.1021/bi00102a019.

APA

George L. Kenyon, John A. Gerlt, P. Lynne Howell, Vincent M. Powers, Rongshi Li, Gregory A. Petsko, & David J. Neidhart. (1991). Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-.ANG. resolution: identification of the active site and possible catalytic residues. Biochemistry, 30, 9264–9273. https://doi.org/10.1021/bi00102a019

Chicago

George L. Kenyon, John A. Gerlt, P. Lynne Howell, Vincent M. Powers, Rongshi Li, Gregory A. Petsko, and David J. Neidhart. 1991. “Mechanism of the Reaction Catalyzed by Mandelate Racemase. 2. Crystal Structure of Mandelate Racemase at 2.5-.ANG. Resolution: Identification of the Active Site and Possible Catalytic Residues.” Biochemistry 30 (September): 9264–73. doi:10.1021/bi00102a019.