1UZ5
The Crystal Structure of molybdopterin biosynthesis moea protein from Pyrococcus horikosii
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-12-15 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 0.97910, 0.97949, 1.000 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 181.375, 181.375, 71.311 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 42.210 - 2.050 |
| R-factor | 0.218 |
| Rwork | 0.218 |
| R-free | 0.24700 |
| Structure solution method | MAD |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.120 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.036 | 0.096 |
| Number of reflections | 43761 | |
| <I/σ(I)> | 23 | 7.8 |
| Completeness [%] | 99.7 | 99.7 |
| Redundancy | 11.4 | 9.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.3 | CRYSTALLIZED FROM 1.1M LI SULFATE, 0.1M ACETATE, PH4., pH 5.30 |
