2V3Y
His361Ala Escherichia coli aminopeptidase P in complex with product
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200H |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-03-04 |
Detector | MARRESEARCH |
Spacegroup name | P 64 2 2 |
Unit cell lengths | 177.132, 177.132, 96.170 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 154.300 - 1.600 |
R-factor | 0.154 |
Rwork | 0.154 |
R-free | 0.16700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wl9 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.304 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | REFMAC |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.100 | 1.690 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.070 | 0.450 |
Number of reflections | 116058 | |
<I/σ(I)> | 21.2 | 3 |
Completeness [%] | 99.9 | 100 |
Redundancy | 7 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 277 | CRYSTALLISED IN 26% PEG 4K, 0.1 M TRIS PH 8.5 AT 277K. SOAKED IN 26% PEG 4K, 0.1 M TRIS PH 8.5, 1 MM MNCL2, 5 MM VAL-PRO-LEU, 10% MPD FOR 60 MIN AT 277K IMMEDIATELY PRIOR TO DATA COLLECTION. |