2FXU
X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-10-27 |
Detector | MARRESEARCH |
Wavelength(s) | 1.000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 60.125, 56.513, 101.652 |
Unit cell angles | 90.00, 94.56, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.350 |
R-factor | 0.17571 |
Rwork | 0.174 |
R-free | 0.20148 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB code: 1J6Z |
RMSD bond length | 0.016 |
RMSD bond angle | 1.605 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.400 |
High resolution limit [Å] | 1.350 | 1.350 |
Rmerge | 0.046 | 0.389 |
Number of reflections | 72741 | |
<I/σ(I)> | 27.6 | 2.6 |
Completeness [%] | 97.5 | 81.4 |
Redundancy | 3.5 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6 | 298 | The bistramide A- actin complex was mixed with the crystallization buffer in 1:1 ratio. The crystallization buffer is 100 mM MES (ph 6.0), 24% (w/v) PEG1500, 70 mM CaCl2, 1mM NaN3, 1mM TCEP., VAPOR DIFFUSION, temperature 298K |