3AA7
Crystal structure of Actin capping protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-02-11 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 53.913, 68.680, 130.086 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.805 - 1.900 |
R-factor | 0.21144 |
Rwork | 0.209 |
R-free | 0.26071 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1izn |
RMSD bond length | 0.016 |
RMSD bond angle | 1.526 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.068 | 0.290 |
Number of reflections | 37190 | |
<I/σ(I)> | 15.56 | 4.92 |
Completeness [%] | 96.2 | 77.7 |
Redundancy | 6.4 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 12.5% PEG 400, 20MM BACL2, 100MM MES-NAOH, PH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |