4M54
The structure of the staphyloferrin B precursor biosynthetic enzyme SbnB bound to N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid and NADH
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-06-18 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 63.116, 63.116, 159.413 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.726 - 2.360 |
R-factor | 0.2269 |
Rwork | 0.223 |
R-free | 0.25810 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.703 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHENIX (1.8.2-1309) |
Refinement software | PHENIX (1.8.2-1309) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 29.730 | 50.000 | 2.400 |
High resolution limit [Å] | 2.360 | 6.400 | 2.360 |
Rmerge | 0.126 | 0.055 | 0.590 |
Number of reflections | 13956 | ||
<I/σ(I)> | 6.5 | ||
Completeness [%] | 99.4 | 96.8 | 98.7 |
Redundancy | 6.9 | 8.1 | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.1 M Hepes, 0.2 M MgCl2, 29-33% PEG 400, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |