7V6U
Crystal structure of bacterial peptidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
Synchrotron site | PAL/PLS |
Beamline | 7A (6B, 6C1) |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-05-22 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 0.9793 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 82.871, 76.825, 58.207 |
Unit cell angles | 90.00, 134.66, 90.00 |
Refinement procedure
Resolution | 41.432 - 2.144 |
R-factor | 0.2026 |
Rwork | 0.198 |
R-free | 0.24770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2k1g |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 41.432 | 41.432 | 2.270 |
High resolution limit [Å] | 2.140 | 6.380 | 2.140 |
Rmerge | 0.103 | 0.043 | 0.493 |
Rmeas | 0.122 | 0.051 | 0.606 |
Total number of observations | 48953 | ||
Number of reflections | 13739 | 561 | 1813 |
<I/σ(I)> | 9.86 | 24.38 | 2.18 |
Completeness [%] | 95.0 | 96.4 | 78.5 |
Redundancy | 3.563 | 3.414 | 2.783 |
CC(1/2) | 0.995 | 0.996 | 0.942 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 7 | 290 | 0.2M DL-Malic acid, 20% PEG 3350 |