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1BVX

THE 1.8 A STRUCTURE OF GEL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]293
Detector technologyIMAGE PLATE
DetectorRIGAKU RAXIS IIC
Spacegroup nameP 43 21 2
Unit cell lengths79.203, 79.203, 38.040
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 1.800
R-factor0.182
Rwork0.182
R-free0.21700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)193l
RMSD bond length0.008
RMSD bond angle22.190

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]99.000
High resolution limit [Å]1.7001.700

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Rmerge0.0680.232

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Total number of observations68445

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Number of reflections12433
<I/σ(I)>21.6
Completeness [%]89.651.8

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Redundancy5.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1liquid-gel diffusion

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4.5HEWL CRYSTALS WERE GROWN IN A GELLED PROTEIN SOLUTION WITH AGAROSE (SIGMA, TYPE VII: OF LOW GELLING TEMPERATURE), 4 % MPD IN ACETATE BUFFER (PH 4.5), THE PRECIPITATING AGENT SOL MPD IN BUFFER. THE GLASS TUBE USED WAS 6 CM TALL WITH AN IN CRYSTALS OF TYPICAL DIMENSIONS $SIM$0.7 $TIMES$ 0.6 $TIM, grown in gelled protein solution with agarose
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111protein25 (mg/ml)
211agarose0.2 (%)
3114 (%)0.68M
411MPD4 (%)
51215 (%)2.57M
612MPD15 (%)

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PDB entries from 2024-05-15

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