4JWP
Crystal structure of Ribosomal-protein-alanine N-acetyltransferase from Brucella melitensis in complex with Acetyl CoA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-02-15 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 72.420, 74.380, 67.550 |
Unit cell angles | 90.00, 91.62, 90.00 |
Refinement procedure
Resolution | 41.580 - 2.000 |
R-factor | 0.1754 |
Rwork | 0.173 |
R-free | 0.22480 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | native structure pdb entry 4J3G |
RMSD bond length | 0.013 |
RMSD bond angle | 1.444 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.5.2) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.050 |
High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
Rmerge | 0.069 | 0.027 | 0.301 |
Number of reflections | 24170 | 282 | 1348 |
<I/σ(I)> | 27.17 | 79.05 | 5.74 |
Completeness [%] | 99.5 | 99 | 95.4 |
Redundancy | 10.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 290 | Microlytics MCSG1, C7: 200mM CaCl2, 100mM Tris pH 8.5, 25% PEG 4000G 3350, BrabA.17352.a.A1.PS01094 at 20mg/ml, 2.5mM CoA, VAPOR DIFFUSION, SITTING DROP, temperature 290K |