Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20 Micromolar ZnSO4 in the buffer. 1mM DTT was used as a reducing agent. Cys221 is oxidized.
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Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20 Micromolar ZnSO4 in the buffer. 1mM DTT was used as a reducing agent. Cys221 is oxidized. Descriptor: BETA-LACTAMASE II, GLYCEROL, SULFATE ION, ... Authors: Davies, A.M, Rasia, R.M, Vila, A.J, Sutton, B.J, Fabiane, S.M. Deposit date: 2004-12-17 Release date: 2005-03-31 Last modified: 2024-11-13 Method: X-RAY DIFFRACTION (2.1 Å) Cite: Effect of Ph on the Active Site of an Arg121Cys Mutant of the Metallo-Beta-Lactamase from Bacillus Cereus: Implications for the Enzyme Mechanism Biochemistry, 44, 2005
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2004-12-17



