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1B5Z

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH3R
Temperature [K]283
Detector technologyIMAGE PLATE
DetectorRIGAKU RAXIS IIC
Spacegroup nameP 21 21 21
Unit cell lengths64.670, 110.300, 43.640
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 2.200
R-factor0.19

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Rwork0.148
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)I56F MUTANT HUMAN LYSOZYME
RMSD bond length0.009
RMSD bond angle1.480
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]100.0001.900
High resolution limit [Å]1.8101.810
Rmerge0.051
Total number of observations68449

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Number of reflections23175
<I/σ(I)>2.4
Completeness [%]79.452.6
Redundancy3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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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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