3AAE
Crystal structure of Actin capping protein in complex with CARMIL fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-23 |
| Detector | ADSC QUANTUM 4r |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 231.153, 104.358, 186.633 |
| Unit cell angles | 90.00, 119.09, 90.00 |
Refinement procedure
| Resolution | 49.700 - 3.300 |
| R-factor | 0.24472 |
| Rwork | 0.243 |
| R-free | 0.27092 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3aa0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.156 |
| Data reduction software | DPS |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.700 | 3.420 |
| High resolution limit [Å] | 3.300 | 3.300 |
| Rmerge | 0.126 | 0.382 |
| Number of reflections | 58413 | |
| <I/σ(I)> | 16.4 | 5.56 |
| Completeness [%] | 99.5 | 99.3 |
| Redundancy | 7.6 | 7.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 14% PEG 3350, 180MM TRI-AMMONIUM CITRATE, 100MM MES-NAOH, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
