Inorganic pyrophosphatase crystals fromThermococcus thioreducensfor X-ray and neutron diffraction
Abstract
Inorganic pyrophosphatase (IPPase) from the archaeon Thermococcus thioreducens was cloned, overexpressed in Escherichia coli, purified and crystallized in restricted geometry, resulting in large crystal volumes exceeding 5 mm3. IPPase is thermally stable and is able to resist denaturation at temperatures above 348 K. Owing to the high temperature tolerance of the enzyme, the protein was amenable to room-temperature manipulation at the level of...
Paper Details
Title
Inorganic pyrophosphatase crystals fromThermococcus thioreducensfor X-ray and neutron diffraction
Published Date
Nov 14, 2012
Journal
Volume
68
Issue
12
Pages
1482 - 1487
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