1T7X
Zn-alpha-2-glycoprotein; refolded CHO-ZAG PEG 400
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-09-28 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.0781 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 122.747, 122.747, 65.124 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.100 |
Rwork | 0.232 |
R-free | 0.29300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1t7v |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
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 | 3.210 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.151 | 0.435 |
Number of reflections | 8738 | |
<I/σ(I)> | 12 | 4 |
Completeness [%] | 93.7 | 98.2 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 7.5 | 298 | Ammonium sulfate, PEG 400, HEPES, pH 7.5, Microbatch, temperature 298.0K |