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1KL1

Crystal Structure of Serine Hydroxymethyltransferase Complexed with Glycine

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2001-06-01
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameP 21 21 2
Unit cell lengths61.266, 106.400, 56.986
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 1.930
Rwork0.170
R-free0.19730

*

Structure solution methodFOURIER SYNTHESIS
Starting model (for MR)1kkj
RMSD bond length0.008
RMSD bond angle0.025
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCCP4
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.000
High resolution limit [Å]1.9301.930
Rmerge0.0430.073
Total number of observations80764

*

Number of reflections27979
<I/σ(I)>22.8
Completeness [%]97.690.2
Redundancy2.882.65
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.525

*

Hepes MPD, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
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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