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1AMH

UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH2R
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1995-12
DetectorRIGAKU
Spacegroup nameP 1 21 1
Unit cell lengths45.920, 49.790, 89.880
Unit cell angles90.00, 97.34, 90.00
Refinement procedure
Resolution100.000 - 2.500
R-factor0.182
Rwork0.182
R-free0.24200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1brb
RMSD bond length0.007
RMSD bond angle26.170

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Data reduction softwarebioteX
Data scaling softwarebioteX
Phasing softwareX-PLOR (3.851)
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]100.0002.600
High resolution limit [Å]2.5202.540

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Rmerge0.1200.296
Number of reflections13312470

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<I/σ(I)>7.72.63
Completeness [%]94.591.9
Redundancy3.13
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

5.64

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CRYSTALLIZED AT 277 K FROM 10 MG/ML PROTEIN SOLUTION USING 22% PEG 3350, 10 MM CACL2 AND 0.15M NH4CL AS PRECIPITANT AT PH=5.6 (0.1 M SODIUM CITRATE).
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21reservoirsodium citrate0.1 (M)
31reservoir10 (mM)
41reservoirPEG335022 (%)
51reservoirammonium chloride0.15 (M)

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PDB entries from 2024-05-15

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