2ASF
Crystal structure of the conserved hypothetical protein Rv2074 from Mycobacterium tuberculosis 1.6 A
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-07-29 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.979571, 1.019691, 1.115869 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 73.395, 73.395, 44.794 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.240 - 1.600 |
R-factor | 0.17992 |
Rwork | 0.179 |
R-free | 0.20397 |
Structure solution method | MAD |
RMSD bond length | 0.021 |
RMSD bond angle | 1.271 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.240 | 1.660 |
High resolution limit [Å] | 1.600 | 1.600 |
Number of reflections | 16283 | |
Completeness [%] | 97.6 | 87.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 298 | 20% PEG 4000, 0.2M sodium citrate, 3% dioxane, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |