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.

Authors: Duda D.; Tu C.; Silverman D.N.; Kalb Gilboa A.Joseph; Agbandje-McKenna M.; McKenna R.

Source: Protein and Peptide Letters, Volume 8, Number 1, February 2001 , pp. 63-67(5)

Publisher: Bentham Science Publishers

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 ? 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

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409751

Publication date: 2001-02-01

• Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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• In this Subject: Anatomy & Physiology
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