6VR7
Structure of a pseudomurein peptide ligase type C from Methanothermus fervidus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-08-05 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.911700 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 97.802, 97.802, 138.351 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.110 - 2.500 |
R-factor | 0.2167 |
Rwork | 0.213 |
R-free | 0.27890 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4cvk |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | MoRDa |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 46.110 | 46.110 | 2.600 |
High resolution limit [Å] | 2.500 | 9.010 | 2.500 |
Rmerge | 0.148 | 0.030 | 0.952 |
Rmeas | 0.160 | 0.033 | 1.025 |
Rpim | 0.060 | 0.014 | 0.377 |
Total number of observations | 170022 | 3554 | 19550 |
Number of reflections | 23904 | 598 | 2648 |
<I/σ(I)> | 13.5 | 42.6 | 2.7 |
Completeness [%] | 99.8 | 98.9 | 100 |
Redundancy | 7.1 | 5.9 | 7.4 |
CC(1/2) | 0.990 | 0.979 | 0.824 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 294 | 0.2 M lithium sulfate, 0.1 M Bis-Tris, pH 5.5, 25% w/v PEG3350, 0.33% w/v 1,5-naphthalenedisulfonic acid disodium salt, 0.33% w/v 2,5-pyridinedicarboxylic acid, 0.33% w/v3,5-dinitrosalicylic acid, 0.02 M HEPES sodium, pH 6.8 |