1AM9
HUMAN SREBP-1A BOUND TO LDL RECEPTOR PROMOTER
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1996-10-24 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 94.630, 94.630, 459.100 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 6.000 - 2.300 |
R-factor | 0.219 |
Rwork | 0.219 |
R-free | 0.27800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MAX-DNA STRUCTURE |
RMSD bond length | 0.013 |
RMSD bond angle | 23.770 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.480 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.071 * | |
Number of reflections | 48155 | |
<I/σ(I)> | 36 | |
Completeness [%] | 86.9 * | 52.4 |
Redundancy | 12 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | PROTEIN WAS CRYSTALLIZED FROM 20 % MPD, 100 MM KCL, 20 MM MGCL2, 100 MM HEPES, PH 5.6, VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents
ID | crystal ID | solution ID | reagent name | concentration | details |
1 | 1 | 1 | WATER | ||
10 | 1 | 3 | WATER | ||
11 | 1 | 3 | KCL | ||
12 | 1 | 3 | MGCL2 | ||
13 | 1 | 3 | MES | ||
14 | 1 | 3 | PEG 4000 | ||
15 | 1 | 3 | MPD | ||
2 | 1 | 1 | KCL | ||
3 | 1 | 1 | MGCL2 | ||
4 | 1 | 1 | TRIS-HCL | ||
5 | 1 | 2 | WATER | ||
6 | 1 | 2 | MPD | ||
7 | 1 | 2 | KCL | ||
8 | 1 | 2 | MGCL2 | ||
9 | 1 | 2 | MES |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 0.5 (mM) | |
2 | 1 | reservoir | 150 (mM) | ||
3 | 1 | reservoir | 20 (mM) | ||
4 | 1 | reservoir | MES | 100 (mM) | pH5.6 |
5 | 1 | reservoir | MPD | 10 (%) |