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Status |
Public on Mar 11, 2019 |
Title |
The DNA-binding protein HTa from Thermoplasma acidophilum is an archaeal histone analog |
Organisms |
Escherichia coli; Thermoplasma acidophilum; synthetic construct |
Experiment type |
Expression profiling by high throughput sequencing Genome binding/occupancy profiling by high throughput sequencing
|
Summary |
This SuperSeries is composed of the SubSeries listed below.
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Overall design |
Refer to individual Series
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Citation(s) |
31710291 |
Submission date |
Mar 01, 2019 |
Last update date |
Dec 03, 2019 |
Contact name |
Tobias Warnecke |
E-mail(s) |
molecular.systems.laboratory@gmail.com
|
Organization name |
Imperial College
|
Street address |
Du Cane Road
|
City |
London |
ZIP/Postal code |
W12 0NN |
Country |
United Kingdom |
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Platforms (3) |
GPL18133 |
Illumina HiSeq 2500 (Escherichia coli) |
GPL19604 |
Illumina HiSeq 2500 (synthetic construct) |
GPL26243 |
Illumina HiSeq 2500 (Thermoplasma acidophilum) |
|
Samples (51)
|
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This SuperSeries is composed of the following SubSeries: |
GSE127726 |
The DNA-binding protein HTa from Thermoplasma acidophilum is an archaeal histone analog (RNA-Seq) |
GSE127727 |
The DNA-binding protein HTa from Thermoplasma acidophilum is an archaeal histone analog (Mnase-Seq) |
GSE138576 |
The DNA-binding protein HTa from Thermoplasma acidophilum is an archaeal histone analog (Mnase-seq and EMSA-seq) |
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Relations |
BioProject |
PRJNA525121 |