Experimental procedure
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1995-03 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 58.900, 64.300, 95.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.200 - 2.300 |
R-factor | 0.194 |
Rwork | 0.194 |
R-free | 0.26800 |
Structure solution method | MIR |
RMSD bond length | 0.010 |
RMSD bond angle | 1.500 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | X-PLOR (3.851) |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.200 | 2.360 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.128 | 0.282 |
Total number of observations | 63555 * | |
Number of reflections | 15604 | |
<I/σ(I)> | 4.6 | 2.5 |
Completeness [%] | 93.5 | 98 * |
Redundancy | 4.1 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | PROTEIN WAS CRYSTALLIZED FROM 12% PEG 600, 6% ISOPROPANOL, 100 MM TRIS, PH 8.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7.5 (mg/ml) | |
2 | 1 | drop | beta-octylglucoside | 0.1 (%(w/v)) | |
3 | 1 | drop | Ap4A | 5 (mM) | |
4 | 1 | reservoir | PEG4000 | 17 (%(w/v)) | |
5 | 1 | reservoir | 2-propanol | 8 (%(v/v)) | |
6 | 1 | reservoir | Tris-HCl | 70 (mM) |