4A0F
Structure of selenomethionine substituted bifunctional DAPA aminotransferase-dethiobiotin synthetase from Arabidopsis thaliana in its apo form.
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-09-25 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 233.670, 75.970, 88.630 |
| Unit cell angles | 90.00, 109.20, 90.00 |
Refinement procedure
| Resolution | 41.849 - 2.714 |
| R-factor | 0.2027 |
| Rwork | 0.200 |
| R-free | 0.26100 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.236 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.330 | 2.780 |
| High resolution limit [Å] | 2.720 | 2.710 |
| Rmerge | 0.080 | 0.480 |
| Number of reflections | 76488 | |
| <I/σ(I)> | 12.88 | 2.11 |
| Completeness [%] | 98.2 | 89.5 |
| Redundancy | 3.56 | 2.93 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BISTRIS 0.1 M PH 5.9, 0.2 M LISO4, 15 % PEG3350, DTT |
