3RPT
Crystal structure of the anti-HIV b12 scaffold protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 200 |
Detector technology | CCD |
Collection date | 2009-06-03 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1 |
Spacegroup name | P 1 |
Unit cell lengths | 45.867, 46.240, 62.282 |
Unit cell angles | 78.57, 81.80, 61.11 |
Refinement procedure
Resolution | 26.207 - 1.303 |
R-factor | 0.175 |
Rwork | 0.173 |
R-free | 0.20200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.251 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.310 |
High resolution limit [Å] | 1.290 | |
<I/σ(I)> | 3 | |
Completeness [%] | 79.7 | 76.9 |
Redundancy | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 293 | 0.2 M Li2SO4,0.1 M MgSO4, 0.1 M acetate pH 4.5, and 5% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 293K |