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1KCM

Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]100
Detector technologyCCD
Collection date1999-12-09
DetectorADSC QUANTUM 4r
Wavelength(s)0.9322
Spacegroup nameP 32 2 1
Unit cell lengths50.464, 50.464, 216.105
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 2.000
R-factor0.216

*

Rwork0.216
R-free0.27300

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1FVZ
RMSD bond length0.012
RMSD bond angle1.420

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.060
High resolution limit [Å]1.9901.990
Rmerge0.0510.171
Total number of observations231585

*

Number of reflections220602012

*

<I/σ(I)>25.77.3
Completeness [%]96.791.1
Redundancy4.33

*

2.70

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.2

*

4

*

11% PEG 6000, 0.2M calcium acetate, 100MM cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein14 (mg/ml)
21dropTris-HCl10 (mM)pH7.2
31dropbeta-mercaptoethanol10 (mM)
41reservoirPEG600011 (%(w/v))
51reservoircalcium acetate200 (mM)
61reservoircacodylate100 (mM)pH6.5

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