5H02
Crystal structure of Methanohalophilus portucalensis glycine sarcosine N-methyltransferase tetramutant (H21G, E23T, E24N, L28S)
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 | 2014-06-15 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 1.00000 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 51.874, 120.803, 131.301 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.888 - 1.776 |
R-factor | 0.1775 |
Rwork | 0.176 |
R-free | 0.19580 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5hil |
RMSD bond length | 0.006 |
RMSD bond angle | 0.796 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX (1.8_1069) |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.820 |
High resolution limit [Å] | 1.776 | 1.780 |
Number of reflections | 40112 | |
<I/σ(I)> | 31.518 | |
Completeness [%] | 100.0 | |
Redundancy | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.3 | 277.15 | Protein solution: GSMT (6.6 mg/ml) in 100 mM TES pH 7.3, 2 M KCl, 1 mM EDTA, 1 mM 2-Mercaptoethanol, 0.1 mM SAH and 50 mM glycine. Crystallization reagent: 0.2 M Ammonium phosphate monobasic. 0.23 M ammonia phosphate monobasic, 0.1 mM SAH and 3.35 M betaine were used as cryoprotectant before data collection |