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2XPZ

Structure of native yeast LTA4 hydrolase

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsMAX II BEAMLINE I711
Synchrotron siteMAX II
BeamlineI711
Temperature [K]100
Detector technologyCCD
DetectorMARRESEARCH
Spacegroup nameP 21 21 21
Unit cell lengths70.833, 98.096, 99.197
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution14.981 - 2.300
R-factor0.193
Rwork0.190
R-free0.26910
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)MODEL NATIVE SCLTA4 P3221
RMSD bond length0.008
RMSD bond angle1.117
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwarePHENIX ((PHENIX.REFINE))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.350
High resolution limit [Å]2.3002.300
Rmerge0.0900.240
Number of reflections29531
<I/σ(I)>5.21.4
Completeness [%]94.886
Redundancy2.21.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1LIQUID DIFFUSIONTHE CRYSTALS ARE GROWN IN LIQUID-LIQUID DIFFUSION EXPERIMENTS USING MELTING POINT CAPILLARIES IN WHICH 5 UL PROTEIN (6 MG/ML) IN 10 MM TRIS PH 8.5 IS LAYERED ON 5 UL 14% PEG 8000 AND 100 MM TRIS PH 7.3.

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PDB entries from 2024-11-06

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