3ZXP
Structural and Functional Analyses of the Bro1 Domain Protein BROX
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-08-14 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 228.064, 67.164, 103.865 |
| Unit cell angles | 90.00, 96.95, 90.00 |
Refinement procedure
| Resolution | 27.374 - 2.495 |
| R-factor | 0.2037 |
| Rwork | 0.201 |
| R-free | 0.24740 |
| Structure solution method | MAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.724 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.060 | 0.480 |
| Number of reflections | 54427 | |
| <I/σ(I)> | 21.9 | 2.6 |
| Completeness [%] | 97.7 | 96.5 |
| Redundancy | 3.7 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.6 | 22% PEG 1500, 0.1M MMT 6.6 |
