1BZH
Cyclic peptide inhibitor of human PTP1B
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 39.690, 86.820, 52.000 |
Unit cell angles | 90.00, 96.91, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.100 |
R-factor | 0.211 * |
Rwork | 0.196 |
R-free | 0.26200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2hnp |
RMSD bond length | 0.010 |
RMSD bond angle | 0.034 |
Data reduction software | DENZO |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 8.000 | 2.210 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.029 | 0.074 |
Total number of observations | 46108 * | |
Number of reflections | 15934 | |
<I/σ(I)> | 13.7 | 8.8 |
Completeness [%] | 78.1 | 55.7 |
Redundancy | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | 4 * | pH 8.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG4000 | 16 (%(w/v)) | |
2 | 1 | reservoir | 0.2 (M) | ||
3 | 1 | reservoir | HEPES | 0.1 (M) | |
4 | 1 | drop | protein | 10 (mg/ml) | |
5 | 1 | drop | FOMT | 5 (mM) |