In:
Acta Crystallographica Section F Structural Biology Communications, International Union of Crystallography (IUCr), Vol. 75, No. 4 ( 2019-04-01), p. 307-311
Abstract:
The hyperthermophilic crenarchaeon Ignicoccus hospitalis KIN4/I possesses at least 35 putative genes encoding enzymes that belong to the α/β-hydrolase superfamily. One of those genes, the metallo-hydrolase-encoding igni18 , was cloned and heterologously expressed in Pichia pastoris . The enzyme produced was purified in its catalytically active form. The recombinant enzyme was successfully crystallized and the crystal diffracted to a resolution of 2.3 Å. The crystal belonged to space group R 32, with unit-cell parameters a = b = 67.42, c = 253.77 Å, α = β = 90.0, γ = 120.0°. It is suggested that it contains one monomer of Igni18 within the asymmetric unit.
Type of Medium:
Online Resource
ISSN:
2053-230X
DOI:
10.1107/S2053230X19002851
DOI:
10.1107/S2053230X19002851/or5014sup1.pdf
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2019
detail.hit.zdb_id:
2175956-X
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