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1B1X

STRUCTURE OF DIFERRIC MARE LACTOFERRIN AT 2.62A RESOLUTION

Replaces:  1BGR
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]288
Detector technologyIMAGE PLATE
Collection date1997-03-15
DetectorMARRESEARCH
Spacegroup nameP 21 21 21
Unit cell lengths85.175, 99.496, 103.052
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 2.620
R-factor0.194

*

Rwork0.194
R-free0.26400
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)HUMAN LACTOFERRIN
RMSD bond length0.012
RMSD bond angle2.000
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.780
High resolution limit [Å]2.6202.620
Rmerge0.0630.250
Number of reflections25558
<I/σ(I)>28.75.29
Completeness [%]95.380

*

Redundancy3.873.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Microdialysis

*

8.56

*

40MG/ML PROTEIN IN 10MM TRIS HCL, PH 8.5, MICRODIALYSED AGA AT 6 DEGREES CELSIUS
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111protein20-30 (mg/ml)
211Tris-HCl0.025 (M)
312ethanol10 (%(v/v))

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PDB entries from 2024-05-15

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