2V6Y
Structure of the MIT domain from a S. solfataricus Vps4-like ATPase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | I 21 21 21 |
Unit cell lengths | 56.178, 69.267, 123.184 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 61.660 - 2.400 |
R-factor | 0.253 |
Rwork | 0.252 |
R-free | 0.27700 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.012 |
RMSD bond angle | 1.333 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SnB |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 61.500 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.070 | 0.370 |
Number of reflections | 27901 | |
<I/σ(I)> | 10.3 | 1.9 |
Completeness [%] | 99.0 | 99 |
Redundancy | 3.6 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | RESERVOIR: 0.6 M AMMONIUM TARTRATE AND 2% PEG4K PROTEIN SOLUTION: 9 MG/ML IN 20 MM TRIS PH 8, 100 MM NACL, 2MM DTT |