2VFO
Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125L
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 | 2006-10-29 |
Detector | MARRESEARCH |
Spacegroup name | P 21 3 |
Unit cell lengths | 120.270, 120.270, 120.270 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.500 |
R-factor | 0.123 |
Rwork | 0.122 |
R-free | 0.14400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tyv |
RMSD bond length | 0.009 |
RMSD bond angle | 1.263 |
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 | 0.040 | 0.100 |
Number of reflections | 76307 | |
<I/σ(I)> | 32.2 | 8.9 |
Completeness [%] | 98.1 | 90.6 |
Redundancy | 9.3 | 2.5 |
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 |