5VC2
Crystal structure of a serine hydroxymethyltransferase from Helicobacter pylori
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-03-22 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.970, 91.020, 161.320 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.813 - 1.900 |
R-factor | 0.1655 |
Rwork | 0.165 |
R-free | 0.19920 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3n0l |
RMSD bond length | 0.007 |
RMSD bond angle | 0.780 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX (dev_2719) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 41.813 | 41.813 | 1.950 |
High resolution limit [Å] | 1.900 | 8.500 | 1.900 |
Rmerge | 0.053 | 0.024 | 0.570 |
Rmeas | 0.060 | 0.027 | 0.639 |
Number of reflections | 67402 | 812 | 4954 |
<I/σ(I)> | 17.07 | 40.59 | 2.67 |
Completeness [%] | 98.9 | 92.7 | 100 |
Redundancy | 4.889 | 4.405 | 4.99 |
CC(1/2) | 0.999 | 0.999 | 0.827 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | HepyC.00008.a.B1.PS38187 at 21.07 mg/mL against Morpheus screen condition F10: 10% PEG 8000, 20% ethylene glycol, 0.02 M D-glucose, 0.02 M D-mannose, 0.02 M D-galactose, 0.02 M L-fucose, 0.02 M D-xylose, 0.02 M N-acetyl-D-glucosamine, 0.1 M bicine/Trizma pH 8.5 |