3SLZ
The crystal structure of XMRV protease complexed with TL-3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-10-20 |
Detector | marccd 300 |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.483, 65.546, 69.732 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.780 - 1.400 |
R-factor | 0.17628 |
Rwork | 0.176 |
R-free | 0.20144 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.765 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASES |
Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.450 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.438 | |
Number of reflections | 42500 | |
<I/σ(I)> | 42.7 | 2.77 |
Completeness [%] | 99.2 | 95.5 |
Redundancy | 7.3 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 3.5M NaFormat, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |