1KQ4
CRYSTAL STRUCTURE OF A THY1-COMPLEMENTING PROTEIN (TM0449) FROM THERMOTOGA MARITIMA AT 2.25 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 | 2001-05-30 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.200, 116.610, 141.830 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.250 |
R-factor | 0.192 |
Rwork | 0.192 |
R-free | 0.24000 |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.270 |
High resolution limit [Å] | 2.250 | 2.250 |
Number of reflections | 43752 | |
<I/σ(I)> | 10.6 | |
Completeness [%] | 99.1 | 100 |
Redundancy | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 | 293 | 50% (v/v)PEG-200, 0.1M HEPES pH7.5, final pH7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |