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1HO3

CRYSTAL STRUCTURE ANALYSIS OF E. COLI L-ASPARAGINASE II (Y25F MUTANT)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineX11
Temperature [K]290
Detector technologyIMAGE PLATE
Collection date1995-12-10
DetectorMARRESEARCH
Wavelength(s)0.98
Spacegroup nameP 65 2 2
Unit cell lengths80.999, 80.999, 341.075
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution10.000 - 2.500
R-factor0.182

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Rwork0.182
R-free0.24500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3eca
RMSD bond length0.008
RMSD bond angle1.400
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.540
High resolution limit [Å]2.4502.450
Rmerge0.0970.364
Total number of observations74462

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Number of reflections23517
<I/σ(I)>7.92
Completeness [%]92.087

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Redundancy3.171.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

4.820

*

Kozak, M., (2000) Acta Biochim. Pol., 47, 807.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10-15 (mg/ml)
21dropsodium citrate10 (mM)
31reservoirMPD46-48 (%)
41reservoirsodium citrate100 (mM)
51reservoir10-20 (mM)

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