2BM4
The Structure of MfpA (Rv3361c, C2 Crystal form). The Pentapeptide Repeat Protein from Mycobacterium tuberculosis Folds as A Right- handed Quadrilateral Beta-helix.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 93 |
| Detector technology | IMAGE PLATE |
| Detector | MSC RAXIS IV |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 177.180, 31.109, 69.601 |
| Unit cell angles | 90.00, 111.45, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.200 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.26400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PREVIOUS STRUCTURE DETERMINED BY SE-MET MAD |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.950 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.030 | 0.130 |
| Number of reflections | 17270 | |
| <I/σ(I)> | 19.8 | 5.8 |
| Completeness [%] | 93.3 | 85.5 |
| Redundancy | 2.6 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 * | PROTEIN WAS CRYSTALLIZED FROM 20% PEG 400, 100 MM AMMONIUM CITRATE PH 5.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5-10 (mg/ml) | |
| 2 | 1 | drop | Tris | 10 (mM) | |
| 3 | 1 | drop | ethylene glycol | 1 (%) | |
| 4 | 1 | drop | beta-mercaptoethanol | 30 (mM) | |
| 5 | 1 | reservoir | PEG400 | 30 (%) | |
| 6 | 1 | reservoir | ammonium citrate | 100 (mM) |
