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
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F16%3A00469849" target="_blank" >RIV/61388971:_____/16:00469849 - isvavai.cz</a>
Alternative codes found
RIV/60076658:12310/16:43891107 RIV/60076658:12520/16:43891107
Result on the web
<a href="http://dx.doi.org/10.1107/S2053230X16011626" target="_blank" >http://dx.doi.org/10.1107/S2053230X16011626</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S2053230X16011626" target="_blank" >10.1107/S2053230X16011626</a>
Alternative languages
Result language
angličtina
Original language name
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
Original language description
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(1), with unit-cell parameters a = 83.42, b = 176.58, c = 126.03 angstrom, alpha = beta = gamma = 90.00 degrees and two molecules in the asymmetric unit (V-M = 2.55 angstrom(3) Da(-1), solvent content 50.47%). X-ray diffraction data were collected to a resolution of 2.45 angstrom.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
ISSN
2053-230X
e-ISSN
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Volume of the periodical
72
Issue of the periodical within the volume
9
Country of publishing house
GB - UNITED KINGDOM
Number of pages
5
Pages from-to
672-676
UT code for WoS article
000384167800003
EID of the result in the Scopus database
2-s2.0-84986269515