1GTN
Structure of the trp RNA-binding attenuation protein (TRAP) bound to an RNA molecule containing 11 GAGCC repeats
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 120 |
Collection date | 1999-02-15 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 145.839, 111.722, 138.715 |
Unit cell angles | 90.00, 117.78, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.500 |
R-factor | 0.235 * |
Rwork | 0.235 |
R-free | 0.27300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gtf |
RMSD bond length | 0.019 * |
RMSD bond angle | 2.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.07) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.050 | 0.265 |
Number of reflections | 65753 | 5337 * |
<I/σ(I)> | 13.5 | 2.4 |
Completeness [%] | 94.6 | 77 |
Redundancy | 1.8 | 1.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.8 * | 0.2M K-GLUTAMATE, 50MM TRIETHANOLAMINE PH8.0,10MM MGCL2, 8-11% MONOMETHYL PEG 2000,+0.4M KCL AT END, pH 8.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein-RNA | 15 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 70 (mM) | pH7.8 |
3 | 1 | drop | L-tryptophan | 10 (mM) | |
4 | 1 | reservoir | potassium glutamate | 0.2 (M) | |
5 | 1 | reservoir | tri-ethanolamine | 50 (mM) | pH8.0 |
6 | 1 | reservoir | 10 (mM) | ||
7 | 1 | reservoir | PEG2000 MME | 8-11 (%) |