1VKU
Crystal structure of Acyl carrier protein (TM0175) from Thermotoga maritima at 2.00 A resolution
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-05-02 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.898407, 0.979608, 0.979462 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 45.420, 45.420, 74.340 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 27.020 - 2.000 |
R-factor | 0.19954 |
Rwork | 0.197 |
R-free | 0.25276 |
Structure solution method | MAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.373 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (4.2)) |
Phasing software | autoSHARP |
Refinement software | REFMAC (5.2.0001) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 27.020 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 6172 | |
<I/σ(I)> | 10.8 | 2.6 |
Completeness [%] | 96.8 | 83.9 |
Redundancy | 5.1 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION,SITTING DROP,NANODROP | 7.7 | 277 | 0.2M MgAcetate, 20% PEG-3350, pH 7.7, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K |