3ZFP
Crystal structure of product-like, processed N-terminal protease Npro with internal His-Tag
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X12 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-12-19 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.390, 41.040, 44.510 |
Unit cell angles | 90.00, 115.31, 90.00 |
Refinement procedure
Resolution | 21.170 - 1.250 |
R-factor | 0.16082 |
Rwork | 0.158 |
R-free | 0.20662 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3zfn |
RMSD bond length | 0.026 |
RMSD bond angle | 2.604 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.500 | 1.320 |
High resolution limit [Å] | 1.250 | 1.250 |
Rmerge | 0.050 | 0.490 |
Number of reflections | 37962 | |
<I/σ(I)> | 12.4 | 2.6 |
Completeness [%] | 98.9 | 97.4 |
Redundancy | 3.7 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 100MM NAACETATE, PH 8.5 25% PEG6000 |