5IAX
Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual Bacterial Prolyl Hydroxylase - Co-BaP4H-PPG
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-01-14 |
Detector | NOIR-1 |
Wavelength(s) | 1.00 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.791, 75.553, 105.768 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 61.479 - 2.100 |
R-factor | 0.1985 |
Rwork | 0.197 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5iat |
RMSD bond length | 0.011 |
RMSD bond angle | 1.082 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.22) |
Phasing software | PHASER |
Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 61.479 | 61.479 | 2.210 |
High resolution limit [Å] | 2.100 | 6.640 | 2.100 |
Rmerge | 0.030 | 0.496 | |
Rmeas | 0.088 | ||
Rpim | 0.041 | ||
Total number of observations | 111271 | ||
Number of reflections | 24447 | ||
<I/σ(I)> | 13.1 | 15.3 | 1.4 |
Completeness [%] | 99.8 | 99.4 | 100 |
Redundancy | 4.6 | 4.2 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.15 M KBr, 30 % PEG 2000 MME |