1UT7
Structure of the conserved domain of ANAC, a member of the NAC family of transcription factors
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 | 2003-04-17 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.365, 75.302, 80.515 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.900 |
R-factor | 0.214 |
Rwork | 0.212 |
R-free | 0.24400 |
Structure solution method | MIRAS |
RMSD bond length | 0.015 |
RMSD bond angle | 1.400 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.061 | 0.307 |
Number of reflections | 26725 | |
<I/σ(I)> | 6.1 | 2.3 |
Completeness [%] | 97.9 | 95.1 |
Redundancy | 4.1 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | Olsen, A., (2004) Acta Crystallogr.,Sect.D, 60, 112. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG4000 | 10-15 (%) | |
2 | 1 | reservoir | imidazole-malic acid | 0.1 (M) | pH7.0 |
3 | 1 | drop | protein | 3.2-7.7 (mg/ml) |