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1E5L

Apo saccharopine reductase from Magnaporthe grisea

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsMAX II BEAMLINE I711
Synchrotron siteMAX II
BeamlineI711
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1999-03-15
DetectorMARRESEARCH
Spacegroup nameC 2 2 21
Unit cell lengths89.330, 119.000, 195.940
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.910 - 2.400
R-factor0.222
Rwork0.222
R-free0.25900
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ff9
RMSD bond length0.007
RMSD bond angle23.100

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareEPMR
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0002.440
High resolution limit [Å]2.4002.400
Rmerge0.0900.335
Total number of observations386685

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Number of reflections40017
<I/σ(I)>243.3
Completeness [%]97.182.2
Redundancy9.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

44

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8 MG/ML PROTEIN, 11-14 % (W/W) PEG6000, 0.1 M CITRIC ACID PH 4.0, 0.1 % BETA-OCTYLGLUCOSIDE, 1 MM DTT
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein8 (mg/ml)
21dropbeta-octylglucoside0.5 (%)
31reservoirPEG600011-14 (%(w/w))
41reservoircitric acid0.1 (M)
51reservoirdithiothreitol1 (mM)

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PDB entries from 2024-05-15

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