1I3F
Ribonuclease T1 V89S mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1999-08-14 |
Detector | MARRESEARCH |
Wavelength(s) | 0.909 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.308, 46.886, 49.901 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.350 |
R-factor | 0.173 * |
Rwork | 0.173 |
R-free | 0.28340 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.493 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.430 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.151 | 0.406 |
Total number of observations | 13465 * | |
Number of reflections | 4178 | |
<I/σ(I)> | 7.11 | 3.13 |
Completeness [%] | 98.6 | 97.7 |
Redundancy | 3.22 | 3.25 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.2 | 293 | Zegers, I., (1998) Nat.Struct.Biol., 5, 280. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | RNase T1 | 15 (mg/ml) | |
2 | 1 | drop | exo-cGPS | 15 (mM) | |
3 | 1 | drop | 20 (mM) | ||
4 | 1 | drop | 2 (mM) | ||
5 | 1 | reservoir | MPD | 55 (%(v/v)) |