4FUK
Aminopeptidase from Trypanosoma brucei
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-06-22 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97625 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 48.385, 75.545, 180.997 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.190 - 1.750 |
R-factor | 0.19593 |
Rwork | 0.194 |
R-free | 0.22891 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2g6p |
RMSD bond length | 0.011 |
RMSD bond angle | 1.382 |
Data reduction software | XDS |
Data scaling software | SCALA (CCP4_3.3.20) |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0027) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.390 | 48.390 | 1.840 |
High resolution limit [Å] | 1.750 | 5.530 | 1.750 |
Rmerge | 0.085 | 0.040 | 0.790 |
Number of reflections | 67991 | ||
<I/σ(I)> | 13.8205 | ||
Completeness [%] | 100.0 | 99.88 | 99.97 |
Redundancy | 7.36 | 6.67 | 7.42 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.5 | 298 | 0.1M Tris pH 6.5, 28% peg 2K MME, vapor diffusion, temperature 298K |