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3TRS

The crystal structure of aspergilloglutamic peptidase from Aspergillus niger

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsPHOTON FACTORY BEAMLINE BL-6A
Synchrotron sitePhoton Factory
BeamlineBL-6A
Spacegroup nameP 21 21 21
Unit cell lengths60.692, 65.842, 77.391
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution38.660 - 1.600
R-factor0.21
Rwork0.208
R-free0.23900
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1y43
RMSD bond length0.019
RMSD bond angle1.925
Data reduction softwareDENZO
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareREFMAC (5.5.0109)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.640
High resolution limit [Å]1.6001.600
Rmerge0.0710.309
Number of reflections37983
<I/σ(I)>12.253.24
Completeness [%]95.985.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP2.72771.3M AMMONIUM SULFATE, 0.1M GLYCINE BUFFER (PH 2.7), 5% (V/V) DMSO, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K

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PDB entries from 2024-06-26

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