3EAF
Crystal structure of ABC transporter, substrate binding protein Aeropyrum pernix
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2008-08-15 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9799 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 41.125, 91.070, 192.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.320 - 2.000 |
R-factor | 0.16691 |
Rwork | 0.165 |
R-free | 0.20651 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.049 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHARP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.320 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.113 | 0.354 |
Number of reflections | 22243 | |
<I/σ(I)> | 17.6 | 6.2 |
Completeness [%] | 88.8 | 74.1 |
Redundancy | 11 | 9.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 25% PEG 1500, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |