1X3O
Crystal structure of the acyl carrier protein from thermus thermophilus HB8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-11-11 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.9 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 93.368, 93.368, 26.047 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.500 |
R-factor | 0.252 |
Rwork | 0.252 |
R-free | 0.28200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1l0h |
RMSD bond length | 0.005 |
RMSD bond angle | 1.100 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.046 | 0.473 |
Number of reflections | 18911 | |
<I/σ(I)> | 16.7 | 4.06 |
Completeness [%] | 98.8 | 96 |
Redundancy | 10.1 | 10.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Gel-Tube | 4.2 | 293 | PEG 4000, dioxane, acetate, pH 4.2, Gel-Tube, temperature 293K |