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1OUC

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH3R
Temperature [K]283
Detector technologyIMAGE PLATE
Collection date1994-10-04
DetectorRIGAKU RAXIS IIC
Spacegroup nameP 21 21 21
Unit cell lengths56.800, 60.910, 33.830
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 1.800
R-factor0.153
Rwork0.153
RMSD bond length0.008
RMSD bond angle23.846

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Data reduction softwareRIGAKU (SOFTWARE)
Data scaling softwareRIGAKU
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 Overall
High resolution limit [Å]1.800
Rmerge0.034
Total number of observations34707

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Number of reflections10973
Completeness [%]95.9
Redundancy3.16
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

4.510

*

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

*

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

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