9ATX
AcpB protein from Bacillus anthracis, N-terminal part
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-04-15 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.546, 63.520, 119.426 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.540 - 2.110 |
| R-factor | 0.20338 |
| Rwork | 0.201 |
| R-free | 0.24552 |
| Structure solution method | SAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.675 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 43.540 | 43.540 | 2.150 |
| High resolution limit [Å] | 2.110 | 5.720 | 2.110 |
| Rmerge | 0.063 | 0.035 | 0.721 |
| Rmeas | 0.070 | 0.038 | 0.915 |
| Rpim | 0.028 | 0.016 | 0.554 |
| Number of reflections | 20624 | 1180 | 744 |
| <I/σ(I)> | 7.8 | 1.08 | |
| Completeness [%] | 97.5 | 99.7 | 74 |
| Redundancy | 5.6 | 5.8 | 2 |
| CC(1/2) | 0.999 | 0.999 | 0.503 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.8 | 277 | 4.3% PEG-3000, 25% PEG-1000, 0.05 M Bicine pH 8.8 |
