3R2E
Dihydroneopterin aldolase/dihydroneopterin triphosphate 2'-epimerase from Yersinia pestis.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-02-24 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 71.716, 71.716, 107.629 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.000 - 2.150 |
| R-factor | 0.2171 |
| Rwork | 0.215 |
| R-free | 0.25530 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o90 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.698 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 31.000 | 50.000 | 2.190 |
| High resolution limit [Å] | 2.150 | 5.830 | 2.150 |
| Rmerge | 0.060 | 0.032 | 0.855 |
| Number of reflections | 7990 | ||
| <I/σ(I)> | 12.6 | 2.05 | |
| Completeness [%] | 99.6 | 95.7 | 100 |
| Redundancy | 6.8 | 5.9 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | 0.2 M calcium chloride, 0.1 M Bis-tris buffer, 45% MPD, 10 mM guanine, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
