5FDA
The high resolution structure of apo form dihydrofolate reductase from Yersinia pestis at 1.55 A
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 | 2010-12-09 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97912 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 60.265, 79.201, 64.321 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.960 - 1.549 |
| R-factor | 0.1587 |
| Rwork | 0.157 |
| R-free | 0.19420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3q1h |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.973 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.580 |
| High resolution limit [Å] | 1.549 | 4.210 | 1.550 |
| Rmerge | 0.046 | 0.028 | 0.688 |
| Rmeas | 0.050 | 0.030 | 0.796 |
| Rpim | 0.018 | 0.011 | 0.391 |
| Total number of observations | 166938 | ||
| Number of reflections | 22728 | ||
| <I/σ(I)> | 16 | ||
| Completeness [%] | 99.9 | 99.7 | 98 |
| Redundancy | 7.3 | 7.3 | 3.9 |
| CC(1/2) | 0.997 | 0.733 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 297 | 0.1 M Sodium Acetate, 3.0 M Sodium chloride |
