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1O69

Crystal structure of a PLP-dependent enzyme

Experimental procedure
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 32-ID
Synchrotron siteAPS
Beamline32-ID
Detector technologyCCD
DetectorMARRESEARCH
Wavelength(s)0.9795
Spacegroup nameP 65
Unit cell lengths151.774, 151.774, 76.986
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.280 - 1.840
Rwork0.185
R-free0.22500
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.018
RMSD bond angle1.500

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA)
Refinement softwareREFMAC (4.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.2201.950
High resolution limit [Å]1.840

*

1.850
Rmerge0.0710.680
Number of reflections84957
<I/σ(I)>20.54
Completeness [%]98.389.6
Redundancy13.97.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7.5285
Crystallization Reagents
IDcrystal IDsolution IDreagent nameconcentrationdetails
111protein9.6mg/ml
212NaCl150mM
312Hepes20mM
412Methionine10mM
512beta-mercaptoethanol1mM
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropHEPES10 (mM)pH7.5
21drop150 (mM)
31dropmethionine10 (mM)
41dropglycerol10 (%)
51dropdithiothreitol5 (mM)
61dropprotein10 (mg/ml)

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PDB entries from 2024-05-01

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