5E7P
Crystal Structure of MSMEG_0858 (Uniprot A0QQS4), a AAA ATPase.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 120 |
Detector technology | CCD |
Collection date | 2008-10-08 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.987 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 86.801, 111.816, 151.705 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.516 - 2.507 |
R-factor | 0.2082 |
Rwork | 0.206 |
R-free | 0.25100 |
Structure solution method | SAD |
RMSD bond length | 0.003 |
RMSD bond angle | 0.770 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (dev_833) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.516 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.487 | |
Number of reflections | 51244 | |
<I/σ(I)> | 15.9 | 2 |
Completeness [%] | 97.5 | 95 |
Redundancy | 4.8 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | purified protein 6.5 mg/ml was mixed with equal volume of 0.3 M ammonium tartrate dibasic and 25% polyethylene glycol 3350. |