1T44
Structural basis of actin sequestration by thymosin-B4: Implications for arp2/3 activation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Wavelength(s) | 1.0052 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.850, 69.335, 80.233 |
Unit cell angles | 90.00, 94.93, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.14709 |
Rwork | 0.144 |
R-free | 0.19531 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1p8z |
RMSD bond length | 0.014 |
RMSD bond angle | 1.434 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.114 | 0.198 |
Number of reflections | 39223 | |
<I/σ(I)> | 11.4 | 3.6 |
Redundancy | 3.3 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 6.5 | 293 | PEG 8000, Sodium acetate, calcium chloride, pH 6.5, microbatch, temperature 293K |