3AA1
Crystal structure of Actin capping protein in complex with the Cp-binding motif derived from CKIP-1
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 | 57.315, 66.298, 136.666 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.360 - 1.900 |
| R-factor | 0.2157 |
| Rwork | 0.213 |
| R-free | 0.26298 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1izn |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.528 |
| 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 | 0.059 | 0.261 |
| Number of reflections | 40661 | |
| <I/σ(I)> | 17.66 | 4.41 |
| Completeness [%] | 97.4 | 81.7 |
| Redundancy | 6.5 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 17.5% PEG 400, 30MM BACL2, 100MM MES-NAOH, PH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
