3SY3
GBAA_1210 protein, a putative adenylate cyclase, from Bacillus anthracis
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 | 2011-06-17 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.322, 85.997, 76.513 |
| Unit cell angles | 90.00, 102.12, 90.00 |
Refinement procedure
| Resolution | 37.280 - 2.140 |
| R-factor | 0.1988 |
| Rwork | 0.196 |
| R-free | 0.24780 |
| Structure solution method | SAD |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.590 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 37.300 | 50.000 | 2.180 |
| High resolution limit [Å] | 2.140 | 5.810 | 2.140 |
| Rmerge | 0.087 | 0.047 | 0.524 |
| Number of reflections | 46815 | ||
| <I/σ(I)> | 9.9 | 2.16 | |
| Completeness [%] | 99.5 | 98.6 | 95.1 |
| Redundancy | 3.8 | 3.4 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 289 | 1 M phosphate buffer, chymotrypsin, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
