1BD9
HUMAN PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX7.2 |
Synchrotron site | SRS |
Beamline | PX7.2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-06-15 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.420, 60.740, 67.640 |
Unit cell angles | 90.00, 102.42, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.050 |
R-factor | 0.171 * |
Rwork | 0.171 |
R-free | 0.23200 |
Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 0.024 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.140 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.058 | 0.120 |
Number of reflections | 23495 | |
<I/σ(I)> | 22.3 | 9.8 |
Completeness [%] | 100.0 | 100 |
Redundancy | 3.5 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 6.5 | PROTEIN WAS CRYSTALLIZED FROM 28-32% PEG 4000/6000/8000, 200-300 MM SODIUM ACETATE, 100MM SODIUM CACODYLATE, PH 6.5; THEN SOAKED IN 28-32% PEG 4000/6000/8000, 200-300 MM SODIUM ACETATE, 100MM BIS-TRIS, PH 6.5. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 5 (mg/ml) | can be replaced by 10mg/ml |
2 | 1 | 1 | Bis-Tris | 5 (mM) | |
3 | 1 | 1 | sodium azide | 0.01 (%) | |
4 | 1 | 2 | PEG4000 | 28-32 (%) | can be replaced by PEG6000 or PEG8000 |
5 | 1 | 2 | sodium acetate | 200-300 (mM) | |
6 | 1 | 2 | sodium azide | 0.01 (%) | |
7 | 1 | 2 | sodium cacodylate | 100 (mM) |