4LB0
Crystal structure of a hydroxyproline epimerase from agrobacterium vitis, target efi-506420, with bound trans-4-oh-l-proline
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-06-12 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9793 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 178.014, 178.014, 49.735 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.165 - 1.700 |
R-factor | 0.1594 |
Rwork | 0.158 |
R-free | 0.19190 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4k8l |
RMSD bond length | 0.010 |
RMSD bond angle | 1.320 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.20) |
Phasing software | AMoRE |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 125.875 | 178.014 | 1.790 |
High resolution limit [Å] | 1.700 | 5.380 | 1.700 |
Rmerge | 0.078 | 0.032 | 0.745 |
Total number of observations | 39677 | 99779 | |
Number of reflections | 88126 | ||
<I/σ(I)> | 18.3 | 21.2 | 1 |
Completeness [%] | 99.9 | 98.7 | 99.9 |
Redundancy | 10.4 | 13 | 7.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | Protein (15 mM Bis-Tris, 500 mM NaCl, 10% glycerol, 5 mM DTT, 200 mM 4-OH PROLINE, TEV Treated, Cleavage Unverified); Reservoir (0.1 M NaAcetate, 25% Peg4000, 8% 2-propanol (MCSG4 H2)); Cryoprotection (Reservoir+20% isopropanaol) , pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |