| Task |
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| WP2.3 |
Library
methods |
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| 2.3.1 |
Identify soluble
domains for complex reconstitution |
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| 2.3.2 |
Develop methods
to minimize size and flexibility |
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| 2.3.3 |
Implement point
mutagenesis for protein solubilisation |
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| 2.3.4 |
Screen synthetic
binding proteins as complex stabilisers |
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| 2.3.5 |
Develop new HTP screens for soluble protein complexes |
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| D2.3.1 |
Implementation of
random mutagenesis |
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| D2.3.2 |
Development of
random library and screening methods |
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| M2.3.1 |
Protocols for the
production of protein components |
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| M2.3.2 |
Publication on
library methodologies for complexes |
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| Task |
Description |
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| WP2.4 |
Biophysical
methods |
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| 2.4.1 |
Comparative
benchmarking of biophysical methods |
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| 2.4.2 |
Screening for
conformational stability of weak complexes |
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| 2.4.3 |
Biophysical
characterisation of complex formation |
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| 2.4.4 |
In vivo complex
characterisation |
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| 2.4.5 |
Provide access to
microfluidics crystallization platform |
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| 2.4.6 |
Hybrid methods
for the determination of structures |
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| D2.4.1 |
Delivery of
stabilization screens |
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| D2.4.2 |
Established protocols for in vivo complex characterisation |
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| D2.4.3 |
Systematic
protocol for hybrid structure determination |
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| D2.4.4 |
Evaluation of
biophysical methods |
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| M2.4.1 |
Proof-of-principle
of limited proteolysis protocols |
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| M2.4.2 |
Benchmarking
screen |
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| M2.4.3 |
Protocol for in vivo complex determination |
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| M2.4.4 |
An operating
cryoEM protocol |
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| M2.4.5 |
Uptake of
microfluidic crystallization technology |
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| Task |
Description |
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| WP2.5 |
X-ray
technologies |
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| 2.5.1 |
Development of
precision sample positioning |
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| 2.5.2 |
Development of
software and hardware for HTP screens |
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| 2.5.3 |
Provision of
dehumidifier at a synchrotron beam-line |
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| D2.5.1 |
Micron-sized
X-ray beam on a beam-line |
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| D2.5.2 |
First device
minimising drift and vibration at the sample |
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| D2.5.3 |
Development of
protocols for comparative crystal screens |
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| D2.5.4 |
Maintenance of
unfrozen crystal in controlled environment |
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| M2.5.1 |
Strategic plan to
solve drift and vibration problems |
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| M2.5.2 |
Control software;
error <100nm at 1Hz feedback frequency |
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| M2.5.3 |
Interim report on
comparative screening of complex crystals |
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| M2.5.4 |
Controlled
delivery of <nanolitre drops on mounted crystals |
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| Task |
Description |
1 |
2 |
3 |
4 |
5 |
6 |
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10 |
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12 |
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15 |
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18 |
| WP2.6 |
NMR technology |
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| 2.6.1 |
NMR technology
for protein-protein interface analysis |
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| 2.6.2 |
Methods using
paramagnetic ions for protein complexes |
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| 2.6.3 |
Software
development for protein-protein docking |
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| D2.6.1 |
NMR pulse
sequences fro heteronuclear signal detection |
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| D2.6.2 |
Improved scoring
functions for protein docking solutions |
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| D2.6.3 |
Bioinformatics
tools for interface predictions |
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| D2.6.4 |
New HADDOCK
version for flexible regions |
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| D2.6.5 |
NMR pulse
sequences for paramagnetic constraints |
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| M2.6.1 |
NMR methodology
for protein-protein interface mapping |
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| M2.6.2 |
Demonstration of
improved software for protein docking |
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| Task |
Description |
1 |
2 |
3 |
4 |
5 |
6 |
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11 |
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15 |
16 |
17 |
18 |
| WP2.7 |
LIMS, data
management and bioinformatics |
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| 2.7.1 |
Extension of data
model for protein complexes |
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| 2.7.2 |
Integration of
target selection tools |
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| 2.7.3 |
Implementation of
web service |
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| 2.7.4 |
Analysis of
multiple sequences using PipeAlign |
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| 2.7.5 |
Extension of data
model for complex bioinformatics data |
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| 2.7.6 |
Development of
LIMS compatible bioinformatics |
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| D2.7.1 |
Extended protein
production data model for complexes |
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| D2.7.2 |
Integrated tools
for target selection |
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| D2.7.3 |
Web services for
LIMS |
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| D2.7.4 |
Extended data
model for bioinformatics |
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| M2.7.1 |
Extended protein
production data model |
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| M2.7.2 |
Functional web
services for LIMS |
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| M2.7.3 |
Bioinformatics
platform available to members |
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