1OJL
Crystal structure of a sigma54-activator suggests the mechanism for the conformational switch necessary for sigma54 binding
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-02-21 |
Detector | MARRESEARCH |
Spacegroup name | P 2 2 21 |
Unit cell lengths | 107.440, 114.740, 187.260 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.000 |
R-factor | 0.25457 |
Rwork | 0.252 |
R-free | 0.30833 |
Structure solution method | SIRAS |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXD |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.060 | 0.440 |
Number of reflections | 46186 | |
<I/σ(I)> | 10.9 | 2.6 |
Completeness [%] | 97.5 | 87.8 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | SITTING DROP VAPOUR DIFFUSION, WELL:100MM HEPES PH8.2 9% ISOPROPANOL, 3% METHANOL, 200MM NACL PROTEIN: 10-12MG/ML ,20MM CHES PH9.5,2MM DTT ,0.1MM EDTA. DROP 1:0.6 PROTEIN:WELL, pH 8.00 |