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1G2W

E177S MUTANT OF THE PYRIDOXAL-5'-PHOSPHATE ENZYME D-AMINO ACID AMINOTRANSFERASE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]277
Detector technologyIMAGE PLATE
Collection date1999-04-29
DetectorRIGAKU RAXIS IIC
Spacegroup nameP 21 21 21
Unit cell lengths77.187, 90.522, 89.097
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution27.000

*

- 2.000
R-factor0.188
Rwork0.188
R-free0.22700
RMSD bond length0.006
RMSD bond angle22.590

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]27.0002.140
High resolution limit [Å]1.8001.800

*

Rmerge0.1230.244

*

Total number of observations303396

*

Number of reflections96070
<I/σ(I)>10
Completeness [%]85.4

*

97.5

*

Redundancy3.23.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.3

*

277resevoir: Tris-HCl, pH 8.5, 22-26% PEG 4K, 0.2-0.4M NaOAc, 1mM alpha-ketoglutarate, enzyme buffer: 50mM KPO4, pH 7.2, 200mM KCl, 1mM DTT, 10uM PLP , VAPOR DIFFUSION, HANGING DROP, temperature 277K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropenzyme30 (mg/ml)
21droppotassium phosphate50 (mM)
31drop0.13 (M)
41dropEDTA0.2 (mM)
51dropPLP50 (mM)
61dropbeta-mercaptoethanol0.01 (%)
71reservoirPEG335026 (%)
81reservoirsodium acetate0.3 (M)
91reservoirTris-HCl0.1 (M)

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