1HA1
HNRNP A1 (RBD1,2) FROM HOMO SAPIENS
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE AREA DETECTOR |
Collection date | 1996-06 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 37.600, 43.500, 55.500 |
Unit cell angles | 90.00, 94.70, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.750 |
R-factor | 0.198 |
Rwork | 0.198 |
R-free | 0.27500 |
Structure solution method | MIR |
RMSD bond length | 0.015 |
RMSD bond angle | 26.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.843) |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.770 |
High resolution limit [Å] | 1.740 | 1.740 |
Rmerge | 0.045 | 0.223 |
Total number of observations | 42714 * | |
Number of reflections | 18507 | |
<I/σ(I)> | 4.3 | 4.1 |
Completeness [%] | 97.1 | 66.2 |
Redundancy | 2.3 | 1.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.1 | 12 * | PROTEIN WAS CRYSTALLIZED FROM 30% PEG 1500, 50 MM NACL, 20 MM TRIS 8.1, THEN MOVED TO 15% ETHYLENE GLYCOL FOR FREEZING. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | RBD1,2 | 18 (mg/ml) | |
2 | 1 | drop | 50 (mM) | ||
3 | 1 | drop | Tris | 30 (mM) | |
4 | 1 | drop | PEG1500 | 14-16 (%) | |
5 | 1 | reservoir | 50 (mM) | ||
6 | 1 | reservoir | Tris | 50 (mM) | |
7 | 1 | reservoir | PEG1500 | 28-32 (%) |