4ZU1
Crystal Structure of O-Acetylserine Sulfhydrylase from Haemophilus influenzae in complex with O-acetyl serine and peptide inhibitor
Replaces: 4MILExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2011-07-13 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.541 |
Spacegroup name | I 41 |
Unit cell lengths | 112.530, 112.530, 43.364 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.202 |
R-factor | 0.2202 |
Rwork | 0.218 |
R-free | 0.25660 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ho1 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.777 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.090 | 0.600 |
Number of reflections | 13806 | |
<I/σ(I)> | 32.9 | 4.71 |
Completeness [%] | 98.9 | 92 |
Redundancy | 5.6 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | o.1 M HEPES 1.2M Sodium Citrate |