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1KTA

HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE : THREE DIMENSIONAL STRUCTURE OF THE ENZYME IN ITS PYRIDOXAMINE PHOSPHATE FORM.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 5.0.2
Synchrotron siteALS
Beamline5.0.2
Temperature [K]223
Detector technologyCCD
Collection date1999-04-20
Spacegroup nameP 21 21 21
Unit cell lengths69.450, 105.308, 107.829
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000

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- 1.900
Rwork0.240
R-free0.28700
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.018
RMSD bond angle24.800

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.930
High resolution limit [Å]1.9001.900
Rmerge0.0570.403
Total number of observations246448

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Number of reflections62273
<I/σ(I)>0.2150.022
Completeness [%]98.491.1
Redundancy1.61.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7

*

Yennawar, N., (2001) Acta Crystallogr., Sect.D, 57, 506.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein2.5 (mg/ml)
21dropHEPES50 (mM)
31dropdithiothreitol20 (mM)
41dropEDTA50 (mM)
51reservoirPEG150022-30 (%)
61reservoirHEPES100 (mM)
71reservoirdithiothreitol20 (mM)

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PDB entries from 2024-05-15

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