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1KKJ

Crystal Structure of Serine Hydroxymethyltransferase from B.stearothermophilus

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2001-02-04
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameP 21 21 2
Unit cell lengths61.154, 106.637, 56.856
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 1.930
Rwork0.178
R-free0.20340

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1dfo
RMSD bond length0.009
RMSD bond angle0.026
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.000
High resolution limit [Å]1.9301.930
Rmerge0.0310.031
Total number of observations68643

*

Number of reflections27746
<I/σ(I)>21.821.8
Completeness [%]97.090.3
Redundancy2.472.29
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.525

*

Hepes MPD, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropHEPES100 (mM)pH7.5
21dropEDTA0.2 (mM)
31drop2-mercaptoethanol5 (mM)
41drop100 (mM)
51dropprotein15 (mg/ml)
61reservoirHEPES100 (mM)pH7.5
71reservoirEDTA0.2 (mM)
81reservoir2-mercaptoethanol5 (mM)
91reservoirMPD50 (%)

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