1USI
L-leucine-binding protein with phenylalanine bound
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Collection date | 2003-03-15 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 68.236, 78.143, 70.183 |
Unit cell angles | 90.00, 102.82, 90.00 |
Refinement procedure
Resolution | 35.000 - 1.800 |
R-factor | 0.191 |
Rwork | 0.189 |
R-free | 0.22200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1usg |
RMSD bond length | 0.025 |
RMSD bond angle | 1.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.19) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | 1.830 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.095 | 0.451 * |
Number of reflections | 60887 | |
<I/σ(I)> | 10.6 | 1.5 |
Completeness [%] | 96.2 | 74 |
Redundancy | 3.1 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 * | 4 * | pH 6.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | pH8.0 |
3 | 1 | reservoir | PEG5000 | 20 (%) | |
4 | 1 | reservoir | sodium acetate | 100 (mM) | pH4.6 |
5 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
6 | 1 | reservoir | 10 (mM) |