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1J49

INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineX11
Temperature [K]298
Detector technologyIMAGE PLATE
Collection date1994-12-01
DetectorMARRESEARCH
Spacegroup nameP 43 21 2
Unit cell lengths79.400, 79.400, 228.500
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000 - 2.200
R-factor0.209
Rwork0.207
R-free0.27100
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2dld
RMSD bond length0.015
RMSD bond angle0.025
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.240
High resolution limit [Å]2.2002.200
Rmerge0.0710.210
Number of reflections38147
<I/σ(I)>19.43.73
Completeness [%]98.793.3
Redundancy5.86.82
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

5pH 5.0
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG2000 Me25 (%)
21reservoirammonium sulfate0.2 (M)
31reservoirNADH5 (mM)
41reservoirsodium acetate0.1 (M)pH5.0

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