1LAR
CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 113 |
Detector technology | CCD |
Collection date | 1997-12 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 66.920, 62.730, 161.590 |
Unit cell angles | 90.00, 98.94, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.222 * |
Rwork | 0.222 |
R-free | 0.27400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1yfo |
RMSD bond length | 0.007 |
RMSD bond angle | 1.330 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.000 |
Rmerge | 0.064 |
Total number of observations | 267242 * |
Number of reflections | 81312 |
<I/σ(I)> | 7 |
Completeness [%] | 91.0 |
Redundancy | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | pH 8.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 100 (mM) | |
3 | 1 | drop | PEG8000 | 8-16 (%(w/v)) | |
4 | 1 | drop | 0.2 (M) |