5IAV
Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual Bacterial Prolyl Hydroxylase - Co-BaP4H-MLI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-11-16 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97860 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.769, 41.495, 111.043 |
Unit cell angles | 90.00, 96.67, 90.00 |
Refinement procedure
Resolution | 29.683 - 1.700 |
R-factor | 0.2124 |
Rwork | 0.211 |
R-free | 0.22890 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5iat |
RMSD bond length | 0.020 |
RMSD bond angle | 1.078 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.683 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.026 | |
Number of reflections | 42773 | |
<I/σ(I)> | 25.5 | 6.6 |
Completeness [%] | 99.6 | 100 |
Redundancy | 3.6 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1 M MIB buffer pH 6.5, 18 % PEG 1500 |