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COMPLEX OF 3'-NEUAC-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH2R
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1996-04-05
DetectorRIGAKU RAXIS IIC
Spacegroup nameC 1 2 1
Unit cell lengths79.100, 85.000, 98.800
Unit cell angles90.00, 107.10, 90.00
Refinement procedure
Resolution10.000 - 2.000
R-factor0.19
Rwork0.190
R-free0.24700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1rtm
RMSD bond length0.007
RMSD bond angle21.900

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR
Refinement softwareX-PLOR (3.54)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]40.0002.070
High resolution limit [Å]2.0002.000
Rmerge0.0600.264
Number of reflections41761
<I/σ(I)>10.63.7
Completeness [%]98.693.2
Redundancy2.42.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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7.822

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8-10% PEG 8000, 2% PEG 1000, 1 MM TRIS-CL, PH 7.8, 200 MM NACL, 20 MM CACL2, 2 MM NAN3. PRIOR TO DATA COLLECTION, THE CRYSTAL WAS ADAPTED TO THE MOTHER LIQUOR PLUS 20% MPD PLUS 80 MM 3'-NEUAC-LEWIS-X.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11drop25 (mM)
101reservoirPEG80008-10 (%(w/v))
111reservoirPEG10002 (%)
121reservoirTris-HCl100 (mM)
131reservoir200 (mM)
141reservoir20 (mM)
151reservoir2 (mM)
21drop2.5 (mM)
31dropprotein1 (mg/ml)
41dropPEG80004-5 (%(w/v))
51dropPEG10001 (%)
61dropTris-HCl50 (mM)
71drop100 (mM)
81drop10 (mM)
91drop1 (mM)

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