2BM6
The Structure of MfpA (Rv3361c, C2221 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 2 2 21 |
Unit cell lengths | 33.393, 48.573, 188.367 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.200 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PREVIOUS STRUCTURE DETERMINED BY SE-MET MAD |
RMSD bond length | 0.020 |
RMSD bond angle | 1.920 |
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 | 0.060 | 0.140 |
Number of reflections | 8004 | |
<I/σ(I)> | 27.7 | 8 |
Completeness [%] | 97.1 | 92.3 |
Redundancy | 6.4 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.5 | PROTEIN (10 MG/ML, 10 MM AMMONIUM CITRATE PH 7.5, 30 MM BETA-MERCAPTOETHANOL) CRYSTALLIZED IN 35% 2-ETHOXYETHANOL, 100 MM CITRATE PH 5.5. CRYSTAL WAS SOAKED IN 100 MM MES PH 5.2, 30 % PEG400, 1 M CESIUM CHLORIDE PRIOR TO VITRIFICATION AND DATA COLLECTION. |