2VFN
Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-05-02 |
Detector | MARRESEARCH |
Spacegroup name | P 21 3 |
Unit cell lengths | 120.437, 120.437, 120.437 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.150 - 1.500 |
R-factor | 0.128 |
Rwork | 0.127 |
R-free | 0.15500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vfq |
RMSD bond length | 0.010 |
RMSD bond angle | 1.338 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.700 |
High resolution limit [Å] | 1.590 | 1.590 |
Rmerge | 0.050 | 0.100 |
Number of reflections | 76620 | |
<I/σ(I)> | 34.9 | 10.2 |
Completeness [%] | 98.1 | 90.5 |
Redundancy | 12.9 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 10 | DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER, 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0 |