Experimental procedure
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 90 |
Detector technology | IMAGE PLATE |
Collection date | 1996-07 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 107.700, 130.200, 81.300 |
Unit cell angles | 90.00, 110.80, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.030 |
R-factor | 0.212 |
Rwork | 0.212 |
R-free | 0.26600 |
RMSD bond length | 0.015 |
RMSD bond angle | 23.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.0) |
Refinement software | X-PLOR (3.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.060 |
High resolution limit [Å] | 2.030 | 2.030 |
Rmerge | 0.082 | 0.173 |
Total number of observations | 563832 * | |
Number of reflections | 125947 | |
<I/σ(I)> | 16 | 6 |
Completeness [%] | 93.4 | 83.8 |
Redundancy | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 8.5 | PROTEIN WAS CRYSTALLIZED USING PRECIPITATING SOLUTION OF 30% PEG 4000, 0.2M NA2MO4, 0.1M TRIS PH 8.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | PEG8000 | 30 (%) | |
2 | 1 | 1 | 0.2 (M) | ||
3 | 1 | 1 | Tris-HCl | 0.1 (M) |