TY  - JOUR
AU  - Grinkevich, Pavel
AU  - Iermak, Iuliia
AU  - Luedtke, Nicholas A.
AU  - Mesters, Jeroen R.
AU  - Ettrich, Rüdiger
AU  - Ludwig, Jost
TI  - pHluorin-assisted expression, purification, crystallization and X-ray diffraction data analysis of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I
JO  - Acta crystallographica / F
VL  - 72
IS  - 9
SN  - 2053-230X
PB  - IUCr
M1  - PUBDB-2016-05653
SP  - 672 - 676
PY  - 2016
N1  - (c) International Union of Crystallography
AB  - The HsdR subunit of the type I restriction-modification system EcoR124I is responsible for the translocation as well as the restriction activity of the whole complex consisting of the HsdR, HsdM and HsdS subunits, and while crystal structures are available for the wild type and several mutants, the C-terminal domain comprising approximately 150 residues was not resolved in any of these structures. Here, three fusion constructs with the GFP variant pHluorin developed to overexpress, purify and crystallize the C-terminal domain of HsdR are reported. The shortest of the three encompassed HsdR residues 887-1038 and yielded crystals that belonged to the orthorhombic space group C222<sub>1</sub>, with unit-cell parameters a = 83.42, b = 176.58, c = 126.03 Å, α = β = γ = 90.00° and two molecules in the asymmetric unit (V<sub>M</sub> = 2.55 Å<sup>3</sup> Da<sup>−1</sup>, solvent content 50.47
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000384167800003
C6  - pmid:27599856
DO  - DOI:10.1107/S2053230X16011626
UR  - https://bib-pubdb1.desy.de/record/315131
ER  -