1WWW
NGF IN COMPLEX WITH DOMAIN 5 OF THE TRKA RECEPTOR
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 160 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 58.245, 53.735, 77.101 |
Unit cell angles | 90.00, 107.34, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.200 |
R-factor | 0.189 * |
Rwork | 0.189 |
R-free | 0.26600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bet |
RMSD bond length | 0.010 |
RMSD bond angle | 1.910 |
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 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.071 * | 0.355 * |
Number of reflections | 23361 | |
<I/σ(I)> | 7.7 | |
Completeness [%] | 99.8 | 98.7 |
Redundancy | 4 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 * | pH 5.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | 0.1 (M) | ||
3 | 1 | drop | bicine | 0.1 (M) | |
4 | 1 | reservoir | PEG3350 | 24 (%) | |
5 | 1 | reservoir | citrate | 0.1 (M) |