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1JFR

CRYSTAL STRUCTURE OF THE STREPTOMYCES EXFOLIATUS LIPASE AT 1.9A RESOLUTION: A MODEL FOR A FAMILY OF PLATELET-ACTIVATING FACTOR ACETYLHYDROLASES

Experimental procedure
Source typeROTATING ANODE
Source detailsENRAF-NONIUS FR591
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1996-07-08
DetectorMACSCIENCE
Spacegroup nameP 1 21 1
Unit cell lengths77.500, 53.000, 81.100
Unit cell angles90.00, 95.80, 90.00
Refinement procedure
Resolution8.000 - 1.900
R-factor0.14

*

Rwork0.140
R-free0.18600
Structure solution methodMIR
RMSD bond length0.016
RMSD bond angle0.028
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHELX-90
Refinement softwareSHELX-90
Data quality characteristics
 Overall
Low resolution limit [Å]20.000
High resolution limit [Å]1.900
Rmerge0.054

*

Total number of observations235302

*

Number of reflections49042
<I/σ(I)>14.75
Completeness [%]95.4
Redundancy4.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7

*

pH 7.75
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropTris-HCl50 (mM)
21dropprotein5.0-7.0 (mg/ml)
31reservoirammonium sulfate30 (%)
41reservoirMME200010 (%)
51reservoirPEG60006 (%)
61reservoirphosphate200 (mM)

221051

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