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1XGO

METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH2R
Temperature [K]289
Detector technologyIMAGE PLATE
Collection date1996-05
DetectorRIGAKU
Spacegroup nameP 62
Unit cell lengths138.916, 138.916, 63.907
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution15.000 - 3.500
R-factor0.182
Rwork0.182
R-free0.27400
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)MONOCLINIC CRYSTAL FORM PDB ENTRY 1XGM
RMSD bond length0.016
RMSD bond angle25.210

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0003.630
High resolution limit [Å]3.5003.500
Rmerge0.1190.265
Total number of observations59765

*

Number of reflections7571
<I/σ(I)>6.11.9
Completeness [%]84.364.9
Redundancy3.65
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

2.6293

*

PROTEIN SOLUTION CONTAINING 16 MG/ML PFMAP, 2 MM COCL2 AND 30 MM L-METHIONINE IN 20 MM POTASSIUM ACETATE AT PH4.5 WAS MIXED WITH EQUAL AMOUNT OF RESERVOIR SOLUTION CONTAINING 10% PEG6000 AND 2.0 M SODIUM CHLORIDE AT PH 2.6, THEN EQUILIBRATED AGAINST RESERVOIR SOLUTION.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG600010 (%(v/v))
21reservoirsodium chloride2.0 (M)

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