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1KL2

Crystal Structure of Serine Hydroxymethyltransferase Complexed with Glycine and 5-formyl tetrahydrofolate

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2001-05-09
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameP 1 21 1
Unit cell lengths57.419, 104.609, 62.489
Unit cell angles90.00, 91.43, 90.00
Refinement procedure
Resolution10.000 - 2.700
Rwork0.208
R-free0.23610

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1kkj
RMSD bond length0.009
RMSD bond angle0.023
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.800
High resolution limit [Å]2.7002.700
Rmerge0.0530.169
Total number of observations53510

*

Number of reflections19264
<I/σ(I)>14.4
Completeness [%]95.397.2
Redundancy2.772.62
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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