4HI1
Crystal structure of acylphosphatase C20R mutant from Vibrio cholerae0395
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2012-07-13 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 39.710, 81.300, 40.530 |
Unit cell angles | 90.00, 90.52, 90.00 |
Refinement procedure
Resolution | 39.708 - 1.964 |
R-factor | 0.1907 |
Rwork | 0.187 |
R-free | 0.24870 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bjd |
RMSD bond length | 0.011 |
RMSD bond angle | 1.328 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.708 | 2.060 |
High resolution limit [Å] | 1.964 | 1.960 |
Rmerge | 0.062 | |
Number of reflections | 17237 | |
<I/σ(I)> | 12.5 | |
Completeness [%] | 93.5 | 93.5 |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 293 | 1.6M ammonium sulfate, 0.1M bicine pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |