1T7V
Zn-alpha-2-glycoprotein; baculo-ZAG PEG 200
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-06-15 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.1271 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 122.878, 122.878, 65.227 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.950 |
Rwork | 0.214 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1zag |
RMSD bond length | 0.011 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.056 | 0.487 |
Number of reflections | 36424 | |
<I/σ(I)> | 20.8 | 2.8 |
Completeness [%] | 99.2 | 98.3 |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 7.5 | 298 | Ammonium sulfate, PEG 200, HEPES, pH 7.5, Microbatch, temperature 298.0K |