5KOI
Crystal Structure of a Possible Enoyl-(acyl-carrier-protein) Reductase from Brucella melitensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-05-27 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97949 |
Spacegroup name | P 1 |
Unit cell lengths | 64.910, 83.830, 106.290 |
Unit cell angles | 90.25, 100.08, 90.82 |
Refinement procedure
Resolution | 48.675 - 1.700 |
R-factor | 0.148 |
Rwork | 0.146 |
R-free | 0.17560 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3grk |
RMSD bond length | 0.006 |
RMSD bond angle | 0.835 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.740 | |
High resolution limit [Å] | 1.700 | 7.600 | 1.700 |
Rmerge | 0.058 | 0.033 | 0.474 |
Number of reflections | 236079 | ||
<I/σ(I)> | 14.19 | 32.92 | 2.91 |
Completeness [%] | 97.2 | 99.3 | 95.6 |
Redundancy | 3.9 | 4 | |
CC(1/2) | 0.998 | 0.997 | 0.898 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 290 | BrabA.00010.c.A1.PS000047 at 18.1 mg/ml, incubated with 4 mM NAD, protein mixed 1:1 and incubated with an equal volume PACT(a6): 25% (w/v) PEG-1500, 10 % (v/v) 10x SPG, pH=9, and cryoprotected with 20% ethylene glycol |