1BKB
INITIATION FACTOR 5A FROM ARCHEBACTERIUM PYROBACULUM AEROPHILUM
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X8C |
Synchrotron site | NSLS |
Beamline | X8C |
Temperature [K] | 110 |
Detector technology | IMAGE PLATE |
Collection date | 1998-05 |
Detector | MARRESEARCH |
Spacegroup name | I 4 |
Unit cell lengths | 114.130, 114.130, 32.590 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.750 |
R-factor | 0.214 |
Rwork | 0.214 |
R-free | 0.23600 |
Structure solution method | MAD |
RMSD bond length | 0.005 |
RMSD bond angle | 25.500 * |
Data reduction software | DENZO |
Data scaling software | CCP4 |
Phasing software | SOLVE |
Refinement software | CNS (0.3) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.830 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.053 * | 0.230 * |
Number of reflections | 21537 * | |
<I/σ(I)> | 8 | 3.3 |
Completeness [%] | 99.8 | 99.3 * |
Redundancy | 7.9 * | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 | 8 * | PROTEIN WAS CRYSTALLIZED AT 8 DEGREES IN 50MM HEPES PH 7.5, 6-8% PEG 4000, 5MM BETA- MERCAPTOETHANOL, temperature 281K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | HEPES | 50 (mM) | |
2 | 1 | 1 | PEG4000 | 5-10 (%) | |
3 | 1 | 1 | dithiothreitol | 5 (mM) | or 5mM beta-mercaptoethanol |