6V7M
Crystal structure of a proteolytically cleaved, amino terminal domain of apolipoprotein E3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR571 |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 1993-06-15 |
Detector | SDMS |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.330, 54.450, 86.670 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.000 - 2.000 |
R-factor | 0.2054 |
Rwork | 0.203 |
R-free | 0.25980 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nfn |
RMSD bond length | 0.006 |
RMSD bond angle | 1.287 |
Data reduction software | SDMS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.330 | 2.060 |
High resolution limit [Å] | 2.000 | 2.010 |
Rmerge | 0.241 | 0.528 |
Rmeas | 0.277 | 0.747 |
Rpim | 0.127 | 0.528 |
Number of reflections | 11748 | 207 |
<I/σ(I)> | 3.9 | 1.1 |
Completeness [%] | 86.0 | |
Redundancy | 3.8 | |
CC(1/2) | 0.968 | 0.096 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.8 | 298 | Crystallization was by sitting drop vapor diffusion in Cryschem plates at room temperature. Reservoirs were 16% to 18 % 2-methyl-2,4-pentanediol (MPD) buffered with 0.1 M sodium acetate at pH 5.8 and including 0.25% octyl-beta-D-1-thioglucopyranoside. The droplets were initial composed of equal amounts of the reservoir and an 8 mg/ml solution of the protein in 0.02 M ammonium carbonate. |