2XMZ
Structure of MenH from S. aureus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2008-09-10 |
Detector | RIGAKU IMAGE PLATE |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 76.548, 43.563, 71.650 |
Unit cell angles | 90.00, 98.26, 90.00 |
Refinement procedure
Resolution | 19.730 - 1.940 |
R-factor | 0.18642 |
Rwork | 0.183 |
R-free | 0.24073 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1r3d |
RMSD bond length | 0.012 |
RMSD bond angle | 1.253 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.730 | 2.050 |
High resolution limit [Å] | 1.940 | 1.940 |
Rmerge | 0.050 | 0.370 |
Number of reflections | 17242 | |
<I/σ(I)> | 17.5 | 3.2 |
Completeness [%] | 98.9 | 93.3 |
Redundancy | 4.1 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | PROTEIN BUFFER: 20 MM TRIS-HCL, 50 MM NACL, PH 7.5. RESERVOIR: 0.1 M NA HEPES PH 7.5, 25 % W/V PEG 4000. |