1WAM
Structure of UDP-galactopyranose mutase from Klebsiella Pneumoniae with FADH-
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 93 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-10-05 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 85.997, 85.997, 100.809 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 27.120 - 2.350 |
| R-factor | 0.204 |
| Rwork | 0.200 |
| R-free | 0.26800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1USJ |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.630 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0007) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.150 | 2.480 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.060 | 0.480 |
| Number of reflections | 18331 | |
| <I/σ(I)> | 9.5 | 1.6 |
| Completeness [%] | 99.6 | 99.1 |
| Redundancy | 2.5 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 0.1M BIS-TRIS PH6.5, 50MM CACL2, 30% PEG550, pH 6.50 |
