8CU9
Crystal Structure of Bifunctional protein GlmU from Klebsiella pneumoniae subsp. pneumoniae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2021-11-11 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 3 |
Unit cell lengths | 139.150, 139.150, 139.150 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.200 - 2.650 |
R-factor | 0.1715 |
Rwork | 0.169 |
R-free | 0.20430 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2oi6 |
RMSD bond length | 0.007 |
RMSD bond angle | 0.881 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MoRDa |
Refinement software | PHENIX (1.20.1-4487) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 49.200 | 49.200 | 2.720 |
High resolution limit [Å] | 2.650 | 11.850 | 2.650 |
Rmerge | 0.048 | 0.025 | 0.637 |
Rmeas | 0.053 | 0.028 | 0.707 |
Total number of observations | 137618 | ||
Number of reflections | 26243 | 309 | 1941 |
<I/σ(I)> | 21.81 | 48.69 | 2.83 |
Completeness [%] | 99.4 | 91.7 | 100 |
Redundancy | 5.244 | 4.505 | 5.308 |
CC(1/2) | 0.999 | 0.998 | 0.819 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 287 | [[Target: KlpnC.00150.a.B1.PW38985] [crystallization: protein at 25.33 mg/mL was mixed 1:1 (0.2 uL protein and 0.2 uL precipitant) with an opt screen based on JCSG+ E1: 0.1 M sodium cacodylate, pH 6.5, 1.0 M tri-sodium citrate] [Barcode: 323500h2] [pin: hnx6-4] [cryo: 20% Ethylene glycol] |