1RP0
Crystal Structure of Thi1 protein from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-01-01 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.28269, 0.915013 |
Spacegroup name | F 2 2 2 |
Unit cell lengths | 102.356, 133.147, 142.301 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 70.710 - 1.600 |
R-factor | 0.14072 |
Rwork | 0.139 |
R-free | 0.17063 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.915 |
Data reduction software | MOSFLM |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.710 | 1.640 |
High resolution limit [Å] | 1.600 | 1.600 |
Number of reflections | 63420 | |
<I/σ(I)> | 16.3 | |
Completeness [%] | 99.4 | 93.6 |
Redundancy | 8.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 291 | TES, magnesium chloride, MES, MPD, heptane-1,2,3-triol, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |