Ultra-High Resolution X-Ray Diffraction From Crystals Of The Kinetic Mutant Of Human Carbonic Anhydrase Ii, His 64 Ala, And Its Complexes With Proton Acceptor Donors.

Author(s): David Duda, Chingkuang Tu, David N. Silverman, A. Joseph Kalb (Gilboa), Mavis Agbandje-McKenna, Robert McKenna.

Journal Name: Protein & Peptide Letters

Volume 8 , Issue 1 , 2001

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Abstract:

Crystals of human carbonic anhydrase II with a specific point mutation, His 64 to Ala, have been grown in a solution of ammonium sulfate in the presence of mercury chloride. The crystals appear in approximately two weeks and belong to the monoclinic space group P21, with unit cell parameters of a = 42.2 A, b = 41.4 A, c = 71.9 A , beta= 104.2 o and one carbonic anhydrase molecule in the asymmetric unit. The crystals diffract X-rays beyond 1.0 Å resolution. These crystals, soaked with exogenous proton acceptor donors, will be used in X-ray and neutron diffraction studies to map the fine water structure “proton wire” in the active site of carbonic anhydrase and to assign the intra- and intermolecular proton transfer pathway(s) from the zinc-bound water out to the bulk solvent.

Keywords: HUMAN CARBONIC, ANHYDRASE II HIS 64 ALA

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Article Details

VOLUME: 8
ISSUE: 1
Year: 2001
Page: [63 - 67]
Pages: 5
DOI: 10.2174/0929866013409751

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