4Q4G
Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-03-03 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9343 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.757, 65.505, 67.978 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.540 - 0.970 |
R-factor | 0.12627 |
Rwork | 0.126 |
R-free | 0.17462 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.028 |
RMSD bond angle | 2.174 |
Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.000 |
High resolution limit [Å] | 0.970 | 0.970 |
Number of reflections | 97211 | |
Completeness [%] | 99.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 5 and 8 mg mL-1 protein concentration, respectively, and 8% (v/v) 2-Propanol, 16% (w/v) PEG4000 in 60 mM Sodium citrate trihydrate buffer, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |