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2BQJ

CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH3R
Temperature [K]283
Detector technologyIMAGE PLATE
Collection date1997-05-09
DetectorRIGAKU RAXIS IIC
Spacegroup nameP 21 21 21
Unit cell lengths56.960, 60.860, 33.500
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 1.800
R-factor0.177
Rwork0.177
Structure solution methodISOMORPHOUS METHOD
Starting model (for MR)C77A/C95A OF HUMAN LYSOZYME
RMSD bond length0.009
RMSD bond angle24.200

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Data reduction softwarePROCESS
Data scaling softwarePROCESS
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]1.900
High resolution limit [Å]1.8001.800
Rmerge0.0360.088
Total number of observations35655

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Number of reflections10303

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<I/σ(I)>8.2
Completeness [%]90.984.5
Redundancy2.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

4.510

*

Takano, K., (1995) J.Mol.Biol., 254, 62.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21reservoir2.5 (M)
31reservoiracetate20 (mM)

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