1YBX
Conserved hypothetical protein Cth-383 from Clostridium thermocellum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9793 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.914, 36.792, 61.824 |
Unit cell angles | 90.00, 111.93, 90.00 |
Refinement procedure
Resolution | 30.964 - 1.800 |
R-factor | 0.22621 |
Rwork | 0.225 |
R-free | 0.25640 |
Structure solution method | SAS |
RMSD bond length | 0.015 |
RMSD bond angle | 1.455 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE (2.06) |
Refinement software | REFMAC (refmac_5.2.0005) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.770 |
High resolution limit [Å] | 1.710 | 3.680 | 1.710 |
Rmerge | 0.063 | 0.047 | 0.396 |
Total number of observations | 2367 | 274 | |
Number of reflections | 16740 | ||
Completeness [%] | 73.3 | 99.8 | 12.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | modified microbatch | 291 | 20% w/v PEG 3350, 0.2M trilithium citrate, modified microbatch, temperature 291K |