3Q3L

The neutron crystallographic structure of inorganic pyrophosphatase from Thermococcus thioreducens

Summary for 3Q3L

• Entry DOI: 10.2210/pdb3q3l/pdb
• Related: 3I98 3Q46 3Q4W 3Q5V 3Q9M
• Descriptor: Tt-IPPase, CALCIUM ION (3 entities in total)
• Functional Keywords: inorganic pyrophosphatase, neutron, phosphatase, hydrolase, pyrophosphatase
• Biological source: Thermococcus thioreducens
• Total number of polymer chains: 6
• Total formula weight: 125525.78

Authors

Hughes, R.C.,Coates, L.,Blakeley, M.P.,Tomanicek, S.J.,Meehan, E.J.,Garcia-Ruiz, J.M.,Ng, J.D. (deposition date: 2010-12-22, release date: 2012-02-08, Last modification date: 2023-09-13)

Primary citation

Hughes, R.C.,Coates, L.,Blakeley, M.P.,Tomanicek, S.J.,Langan, P.,Kovalevsky, A.Y.,Garcia-Ruiz, J.M.,Ng, J.D.
Inorganic pyrophosphatase crystals from Thermococcus thioreducens for X-ray and neutron diffraction.
Acta Crystallogr.,Sect.F, 68:1482-1487, 2012

PubMed 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 protein preparation, crystallization and X-ray and neutron diffraction analyses. A complete synchrotron X-ray diffraction data set to 1.85 Å resolution was collected at room temperature from a single crystal of IPPase (monoclinic space group C2, unit-cell parameters a=106.11, b=95.46, c=113.68 Å, α=γ=90.0, β=98.12°). As large-volume crystals of IPPase can be obtained, preliminary neutron diffraction tests were undertaken. Consequently, Laue diffraction images were obtained, with reflections observed to 2.1 Å resolution with I/σ(I) greater than 2.5. The preliminary crystallographic results reported here set in place future structure-function and mechanism studies of IPPase.

PubMed: 23192028
DOI: 10.1107/S1744309112032447

Experimental method

NEUTRON DIFFRACTION (2.5 Å)