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1B9C

Green Fluorescent Protein Mutant F99S, M153T and V163A

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsELETTRA BEAMLINE 5.2R
Synchrotron siteELETTRA
Beamline5.2R
Temperature [K]100
Detector technologyIMAGE PLATE
DetectorMAR scanner 345 mm plate
Spacegroup nameP 21 21 21
Unit cell lengths83.480, 85.370, 140.060
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000 - 2.400
R-factor0.204
Rwork0.204
R-free0.28000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1gfl
RMSD bond length0.015
RMSD bond angle28.480

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareAMoRE
Refinement softwareX-PLOR (3.8.5)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.640
High resolution limit [Å]2.3702.370
Rmerge0.0620.146
Total number of observations165357

*

Number of reflections367465445

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<I/σ(I)>6.94.2
Completeness [%]83.945
Redundancy4.63.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7.4

*

20

*

22% PEG 4000, 50 MM HEPES PH 8.5, 50 MM MGCL2, 10 MM 2-MERCAPTOETHANOL, 23% MG/ ML PROTEINA, pH 8.3
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein23 (mg/ml)
21dropHEPES10 (mM)
31reservoirPEG400022 (%)
41reservoirHEPES50 (mM)
51reservoir50 (mM)
61reservoir2-mercaptoethanol10 (mM)

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PDB entries from 2024-05-15

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