1YJS
K226Q Mutant Of Serine Hydroxymethyltransferase From B. Stearothermophilus, Complex With Glycine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-03-11 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 61.365, 106.287, 56.981 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.000 |
R-factor | 0.20344 |
Rwork | 0.203 |
R-free | 0.22701 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1kkj |
RMSD bond length | 0.011 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.149 | |
Number of reflections | 25927 | |
<I/σ(I)> | 20.7 | |
Completeness [%] | 97.5 | 98.7 |
Redundancy | 2.4 | 1.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | Hepes, MPD, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |