Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-30 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 96.610, 132.960, 107.830 |
| Unit cell angles | 90.00, 100.11, 90.00 |
Refinement procedure
| Resolution | 29.629 - 2.850 |
| R-factor | 0.205 |
| Rwork | 0.204 |
| R-free | 0.24900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qki |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.190 |
| Data reduction software | TRUNCATE |
| Data scaling software | SCALA (3.3.15) |
| Phasing software | AMoRE |
| Refinement software | BUSTER (2.10.3) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.629 | 29.629 | 3.000 |
| High resolution limit [Å] | 2.850 | 9.010 | 2.850 |
| Rmerge | 0.083 | 0.501 | |
| Rmeas | 0.163 | 0.097 | 0.594 |
| Rpim | 0.086 | 0.050 | 0.316 |
| Number of reflections | 62028 | 1989 | 9028 |
| <I/σ(I)> | 7.1 | 5.9 | 1.5 |
| Completeness [%] | 99.1 | 97.2 | 99.2 |
| Redundancy | 3.5 | 3.7 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 4 microL 20 mg/mL protein (in 20 mM Tris pH8.0, 50mM NaCl, 0.5mM MgCl2), plus 4 microL 6% PEG 400, 1.6 M ammonium sulfate, 0.1 M HEPES pH 7.5 |
