4BPY
Crystal structure of the C90A mutant of the Sco copper chaperone protein from Streptomyces lividans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I24 |
| Synchrotron site | Diamond |
| Beamline | I24 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-01-31 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 32 |
| Unit cell lengths | 41.200, 41.200, 76.631 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.680 - 1.400 |
| R-factor | 0.1335 |
| Rwork | 0.131 |
| R-free | 0.18484 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2b7k |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.863 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.700 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.070 | 0.660 |
| Number of reflections | 28622 | |
| <I/σ(I)> | 10.1 | 2.1 |
| Completeness [%] | 99.8 | 98.5 |
| Redundancy | 3.3 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.5 | 28 % PEG 4000, 0.05 M NAAC PH 4.5 |
