4N03
Fatty acid ABC transporter substrate-binding protein from Thermomonospora curvata
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-07-26 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 63.409, 40.303, 72.557 |
| Unit cell angles | 90.00, 90.60, 90.00 |
Refinement procedure
| Resolution | 35.200 - 1.150 |
| R-factor | 0.125 |
| Rwork | 0.124 |
| R-free | 0.14930 |
| Structure solution method | SAD |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.695 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 35.200 | 50.000 | 1.170 |
| High resolution limit [Å] | 1.150 | 3.120 | 1.150 |
| Rmerge | 0.081 | 0.061 | 0.407 |
| Number of reflections | 123840 | ||
| <I/σ(I)> | 11.8 | 2.24 | |
| Completeness [%] | 94.8 | 99.6 | 66.5 |
| Redundancy | 5.4 | 6.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.1 M Bis-Tris buffer, 2.5 M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
