1XBR
T DOMAIN FROM XENOPUS LAEVIS BOUND TO DNA
Experimental procedure
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-06 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.900, 113.900, 149.000 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.215 |
Rwork | 0.215 |
R-free | 0.28300 |
Structure solution method | MIR |
RMSD bond length | 0.009 |
RMSD bond angle | 24.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.136 * | |
Total number of observations | 101653 * | |
Number of reflections | 22983 | |
<I/σ(I)> | 33.5 | 13.7 |
Completeness [%] | 98.9 | 98.9 |
Redundancy | 4.4 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.2 | PROTEIN WAS CRYSTALLIZED FROM 2-8% PEG 8K, 20 MM MGCL2 50 MM NA-ACETATE, PH 4.2 1MM DTT, 5 MM SPERMINE, VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents
ID | crystal ID | solution ID | reagent name | concentration | details |
1 | 1 | 1 | WATER | ||
10 | 1 | 2 | SPERMINE | ||
2 | 1 | 1 | NACL | ||
3 | 1 | 1 | HEPES | ||
4 | 1 | 1 | DTT | ||
5 | 1 | 2 | WATER | ||
6 | 1 | 2 | PEG 8000 | ||
7 | 1 | 2 | MGCL2 | ||
8 | 1 | 2 | NA ACETATE | ||
9 | 1 | 2 | DTT |