4ONY
Crystal structure of a ABC transporter, periplasmic substrate-binding protein from Brucella melitensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-10-17 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97856 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.560, 124.320, 172.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.100 |
R-factor | 0.15717 |
Rwork | 0.155 |
R-free | 0.19603 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3pam modified with CCP4 program chainsaw |
RMSD bond length | 0.013 |
RMSD bond angle | 1.514 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.5.5) |
Refinement software | REFMAC (5.8.0071) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.150 |
High resolution limit [Å] | 2.100 | 9.390 | 2.100 |
Rmerge | 0.095 | 0.023 | 0.434 |
Number of reflections | 81188 | ||
<I/σ(I)> | 15.02 | 46.46 | 3.15 |
Completeness [%] | 99.3 | 91.7 | 99.8 |
Redundancy | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 290 | RigakuReagents JCSG+ screen, H3: 25% PEG 3350, 100mM BisTris, pH 5.5; cryo 20% EG; BrmeB.17356.a.B2.PS01888 at 17.1mg/ml, tray 248209h3, puck xtp3-5, VAPOR DIFFUSION, SITTING DROP, temperature 290K |