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1G5B

BACTERIOPHAGE LAMBDA SER/THR PROTEIN PHOSPHATASE

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 5ID-B
Synchrotron siteAPS
Beamline5ID-B
Temperature [K]120
Detector technologyCCD
Collection date1999-02-04
DetectorMARRESEARCH
Wavelength(s)0.99188, 1.0098, 1.0247
Spacegroup nameC 2 2 21
Unit cell lengths160.400, 177.300, 79.100
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution35.000 - 2.150
R-factor0.2
Rwork0.200
R-free0.22600
Structure solution methodMAD
RMSD bond length0.006
RMSD bond angle1.200
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.190
High resolution limit [Å]2.1502.150
Rmerge0.0530.316
Total number of observations435477

*

Number of reflections61405
<I/σ(I)>10.62.4
Completeness [%]99.599.6

*

Redundancy44
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6296100 mM MES, 20% PEG 4000, 350 mM Ammonium Sulfate, 10 mM Manganese(II) Chloride, 50 mM Ammonium Acetate, 20 mM Dithiothreitol, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 23K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein19-30 (mg/ml)
21reservoirMES100 (mM)pH6.0
31reservoirammonium sulfate350 (mM)
41reservoirPEG400020 (%)
51reservoirammonium acetate100 (mM)
61reservoir10 (mM)
71reservoirdithiothreitol20 (mM)

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PDB entries from 2025-12-03

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