4NVT
Crystal Structure of Triosephosphate Isomerase from Brucella melitensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-10-24 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.9787 |
Spacegroup name | P 1 |
Unit cell lengths | 51.910, 60.600, 86.170 |
Unit cell angles | 104.57, 99.46, 90.31 |
Refinement procedure
Resolution | 50.000 - 2.100 |
R-factor | 0.1792 |
Rwork | 0.176 |
R-free | 0.23023 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3kxq |
RMSD bond length | 0.013 |
RMSD bond angle | 1.532 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.150 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 57366 | |
<I/σ(I)> | 12.1 | 2.7 |
Completeness [%] | 98.1 | 96.9 |
Redundancy | 3.94 | 3.97 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | MCSG1a11: 10% PEG4K, 0.2M MgCl2, 0.1M Mes pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |