3N5M
Crystals structure of a Bacillus anthracis aminotransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2010-02-12 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97857 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 62.414, 176.176, 80.059 |
| Unit cell angles | 90.00, 94.47, 90.00 |
Refinement procedure
| Resolution | 34.850 - 2.050 |
| R-factor | 0.158 |
| Rwork | 0.156 |
| R-free | 0.19300 |
| Structure solution method | SAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.225 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXS |
| Refinement software | PHENIX (1.6.1_357) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.120 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.097 | 0.604 |
| Number of reflections | 106929 | |
| <I/σ(I)> | 9.7 | 2.2 |
| Completeness [%] | 98.9 | 93.2 |
| Redundancy | 6.8 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | hanging drop | 7 | 298 | 20% PEG 3350,100mM Na Formate,100mM Li Sulfate, 100mM Bis-Tris, pH 7, hanging drop, temperature 298K |
