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5L8S

The crystal structure of a cold-adapted acylaminoacyl peptidase reveals a novel quaternary architecture based on the arm-exchange mechanism

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]100
Detector technologyCCD
Collection date2012-12-11
DetectorADSC QUANTUM 4
Wavelength(s)0.93929
Spacegroup nameP 21 21 21
Unit cell lengths148.080, 151.100, 191.230
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution63.480 - 2.500
R-factor0.21386
Rwork0.212
R-free0.24776
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ve6
RMSD bond length0.009
RMSD bond angle1.282
Data reduction softwareXDS
Data scaling softwareSCALA
Phasing softwarePHASER
Refinement softwareREFMAC (5.7.0032)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]63.7402.640
High resolution limit [Å]2.5002.500
Rmerge0.1280.399
Number of reflections148344
<I/σ(I)>10.84.5
Completeness [%]100.0100
Redundancy5.65.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.527730% PEG 400, 0.1 M Na-Hepes (pH 7.5), and 0.2 M MgCl2

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