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1D0E

CRYSTAL STRUCTURES OF THE N-TERMINAL FRAGMENT FROM MOLONEY MURINE LEUKEMIA VIRUS REVERSE TRANSCRIPTASE COMPLEXED WITH NUCLEIC ACID: FUNCTIONAL IMPLICATIONS FOR TEMPLATE-PRIMER BINDING TO THE FINGERS DOMAIN

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]108
Detector technologyIMAGE PLATE
Collection date1999-05-15
DetectorRIGAKU RAXIS IV
Spacegroup nameP 1 21 1
Unit cell lengths66.160, 63.540, 73.500
Unit cell angles90.00, 103.85, 90.00
Refinement procedure
Resolution20.000

*

- 3.000
R-factor0.215
Rwork0.215
R-free0.29800
RMSD bond length0.011
RMSD bond angle24.460

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]500.0003.110
High resolution limit [Å]3.0003.000
Rmerge0.1490.314
Total number of observations35570

*

Number of reflections11540
<I/σ(I)>5.95
Completeness [%]95.792.2
Redundancy3.12.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5293used to seeding, Sun, D., (1998) Protein Sci., 7, 1575.

*

Crystallization Reagents
IDcrystal IDsolution IDreagent nameconcentrationdetails
111NH4CL
211HEPES
311PEG 4000
412PEG 4000
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirHEPES100 (mM)
21reservoirPEG400013 (%)
31reservoir75 (mM)

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