4RC1
Structure of the methanofuran/methanopterin biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii with PRPP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-06-08 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.03930 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 144.870, 153.030, 132.840 |
| Unit cell angles | 90.00, 111.97, 90.00 |
Refinement procedure
| Resolution | 65.000 - 2.400 |
| R-factor | 0.1938 |
| Rwork | 0.193 |
| R-free | 0.21050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4u9p |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.190 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | BUSTER-TNT |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 65.000 | 10.750 | 2.470 |
| High resolution limit [Å] | 2.400 | 7.600 | 2.400 |
| Rmerge | 0.073 | 0.056 | 0.588 |
| Number of reflections | 102609 | 2070 | 7412 |
| <I/σ(I)> | 9.17 | 18.65 | 2.07 |
| Completeness [%] | 98.3 | 95.4 | 96.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 1.0M (NH4)2 SO4, 20 mM Tris HCl pH 8, 100 mM NaCl, 5% glycerol and 4 mM DTT, vapor diffusion, hanging drop, temperature 298K, VAPOR DIFFUSION, HANGING DROP |
