5I5G
Crystal Structure of Transketolase mutant-R525L from Pichia Stipitis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL15A1 |
Synchrotron site | NSRRC |
Beamline | BL15A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-02-10 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 1.0 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 101.121, 184.543, 98.170 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.560 - 1.950 |
R-factor | 0.1618 |
Rwork | 0.161 |
R-free | 0.18620 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gpu |
RMSD bond length | 0.008 |
RMSD bond angle | 0.902 |
Data scaling software | HKL-2000 |
Refinement software | PHENIX ((1.10_2152: ???)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 1.980 |
High resolution limit [Å] | 1.950 | 5.280 | 1.950 |
Rmerge | 0.155 | 0.049 | 0.946 |
Number of reflections | 67032 | ||
<I/σ(I)> | 5.9 | ||
Completeness [%] | 100.0 | 99.9 | 100 |
Redundancy | 8.3 | 7.9 | 8.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | MES, NaCl, PEG400 |