5HM4
Crystal structure of oligopeptide ABC transporter, periplasmic oligopeptide-binding protein (TM1226) from THERMOTOGA MARITIMA at 2.0 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2013-03-28 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 2 21 |
| Unit cell lengths | 51.256, 65.795, 185.658 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.435 - 2.000 |
| R-factor | 0.1752 |
| Rwork | 0.173 |
| R-free | 0.20860 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vr5 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.654 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.110 | 0.627 |
| Number of reflections | 42275 | |
| <I/σ(I)> | 11.5 | 3.4 |
| Completeness [%] | 97.1 | 96.2 |
| Redundancy | 5.7 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 293 | 0.2-0.3M Mg or Ca Acetate, 20-30% PEG 3350 |
