3KH5
Crystal Structure of Protein MJ1225 from Methanocaldococcus jannaschii, a putative archaeal homolog of g-AMPK.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Collection date | 2009-09-19 |
Spacegroup name | H 3 2 |
Unit cell lengths | 108.548, 108.548, 143.627 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.100 |
R-factor | 0.231 |
Rwork | 0.228 |
R-free | 0.29400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PROTEIN MJ0100 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.768 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 19237 | |
<I/σ(I)> | 45.2 | |
Completeness [%] | 100.0 | |
Redundancy | 24.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 291 | 2.4 M Ammonium sulfate, 2.8 % PEG 400, 100 mM Hepes, 114 mM FOS-choline 8 or 11 mM FOS-choline 10, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |