1AB0
C1G/V32D/F57H MUTANT OF MURINE ADIPOCYTE LIPID BINDING PROTEIN AT PH 4.5
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 1994-06-27 |
Detector | SIEMENS |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 56.470, 56.470, 80.520 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.900 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.25300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lib |
RMSD bond length | 0.007 |
RMSD bond angle | 25.500 * |
Data reduction software | XENGEN |
Data scaling software | XENGEN |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 26.000 | 2.010 |
High resolution limit [Å] | 1.900 | 1.890 |
Rmerge | 0.105 * | |
Total number of observations | 103340 * | |
Number of reflections | 10324 | |
<I/σ(I)> | 8.7 | 0.9 |
Completeness [%] | 97.0 | 65 |
Redundancy | 10.4 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | 2.4M AMSO4 50MM NAKPO4 100 MM ACETATE, PH 4.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | HEPES | 12.5 (mM) | |
2 | 1 | reservoir | protein | 10 (mg/ml) | |
3 | 1 | reservoir | ammonium sulfate | 2.4 (M) | |
4 | 1 | reservoir | 50 (mM) | ||
5 | 1 | reservoir | acetate | 100 (mM) |