3AAA
Crystal Structure of Actin capping protein in complex with V-1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2007-11-14 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 71.424, 87.006, 121.035 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.960 - 2.200 |
| R-factor | 0.18832 |
| Rwork | 0.186 |
| R-free | 0.23696 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1izn |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.419 |
| 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] | 20.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.102 | 0.304 |
| Number of reflections | 38745 | |
| <I/σ(I)> | 24.62 | 7.68 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 14.1 | 13.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.35 | 293 | 10% PEG 4000, 20% ISOPROPANOL, 20MM EDTA, 0.1M TRIS-HCL, pH 8.35, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
