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1UGA

HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY PHE (A65F)

Experimental procedure
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1995-04-01
DetectorRIGAKU RAXIS IIC
Spacegroup nameP 1 21 1
Unit cell lengths42.700, 41.700, 73.000
Unit cell angles90.00, 104.60, 90.00
Refinement procedure
Resolution6.500 - 2.000
R-factor0.154
Rwork0.154
R-free0.24600
Structure solution methodDIFFERENCE FOURIER
Starting model (for MR)NATIVE CAII HAKANSSON ET AL. 1992
RMSD bond length0.009
RMSD bond angle25.300

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Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((AGROVATA)
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]6.5002.360
High resolution limit [Å]2.3002.300
Rmerge0.103

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Total number of observations20445

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Number of reflections10085
<I/σ(I)>6.532
Completeness [%]88.189.7
Redundancy22
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

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8pH 8.0
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropTris-HCl50 (mM)
21dropammonium sulfate1.95-3.9 (M)
31reservoirTris-HCl50 (mM)
41reservoirammonium sulfate1.95-3.9 (M)
51dropenzyme
61dropdithiothreitol2 (mM)

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PDB entries from 2024-11-06

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