2VO9
CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500
Replaces: 1XP2Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-09-24 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 59.787, 95.180, 182.578 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
R-factor | 0.198 |
Rwork | 0.196 |
R-free | 0.24400 |
Structure solution method | SAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.018 |
RMSD bond angle | 1.628 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | HKL2Map |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.060 | 0.240 |
Number of reflections | 46838 | |
<I/σ(I)> | 9.58 | 3.66 |
Completeness [%] | 96.7 | 96.7 |
Redundancy | 3.3 | 3.66 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 0.1M HEPES, 2.4% PEG 400, 1.7M (NH4)2SO4, PH 7.5, VAPOR DIFFUSION, HANGING DROP, 298K |