2PFR
Human N-acetyltransferase 2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-09-07 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 130.063, 130.063, 111.230 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.920 |
Rwork | 0.209 |
R-free | 0.24530 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ija |
RMSD bond length | 0.017 |
RMSD bond angle | 1.405 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (refmac_5.2.0019) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 1.990 |
High resolution limit [Å] | 1.920 | 4.130 | 1.920 |
Rmerge | 0.133 | 0.044 | 0.997 |
Number of reflections | 139603 | 14002 | 13946 |
<I/σ(I)> | 7.9 | ||
Completeness [%] | 100.0 | ||
Redundancy | 7.4 | 7.8 | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 2.5 M Ammonium sulfate, 0.1M TRIS, pH 8.5, vapor diffusion, sitting drop, temperature 291K |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 2.5 M Ammonium sulfate, 0.1M TRIS, pH 8.5, vapor diffusion, sitting drop, temperature 291K |