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1OM9

Structure of the GGA1-appendage in complex with the p56 binding peptide

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2003-01-05
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameP 31 2 1
Unit cell lengths61.414, 61.414, 145.008
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 2.500
R-factor0.21569
Rwork0.213
R-free0.26200

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Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)PDB ID 1NA8 chain A
RMSD bond length0.021
RMSD bond angle1.820

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Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.640
High resolution limit [Å]2.5002.500
Rmerge0.0810.478
Number of reflections11512
<I/σ(I)>16.53.1
Completeness [%]99.999.9
Redundancy4.95
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.5

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288100 mM sodium citrate, 100 mM MgCl2 and 35% PEG 400, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 288K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirsodium citrate100 (mM)pH5.5
21reservoir100 (mM)
31reservoirPEG40035 (%(w/v))
41dropHEPES5 (mM)pH7.5
51drop100 (mM)

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