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24BT

Crystal structure of Peptidyl-tRNA Hydrolase 2 from Candidatus Lokiarchaeum sp. GC14_75

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsPHOTON FACTORY BEAMLINE BL-17A
Synchrotron sitePhoton Factory
BeamlineBL-17A
Temperature [K]95
Detector technologyPIXEL
Collection date2024-10-22
DetectorDECTRIS EIGER X 16M
Wavelength(s)0.98
Spacegroup nameC 1 2 1
Unit cell lengths72.930, 42.174, 156.520
Unit cell angles90.00, 90.12, 90.00
Refinement procedure
Resolution39.130 - 2.120
R-factor0.20028
Rwork0.199
R-free0.21992
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.007
RMSD bond angle1.354
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwareBALBES
Refinement softwareREFMAC (5.8.0419)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]39.1302.250
High resolution limit [Å]2.1202.120
Rmerge0.0530.169
Number of reflections267284253
<I/σ(I)>15
Completeness [%]97.3
Redundancy3.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP29350 mM HEPES-NaOH pH 7.4, 19% (w/v) PEG3350, and 0.2 M Ammonium citrate dibasic

259693

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