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1GAI

GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE

Experimental procedure
Source typeROTATING ANODE
Source detailsSIEMENS
Temperature [K]293
Detector technologyAREA DETECTOR
Collection date1993-10-20
DetectorSIEMENS
Spacegroup nameP 21 21 21
Unit cell lengths116.900, 104.400, 48.400
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 1.700
R-factor0.147
Rwork0.147
R-free0.16700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)NATIVE GLOCOAMYLASE
RMSD bond length0.008
RMSD bond angle21.600

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Data reduction softwareXENGEN
Data scaling softwareXENGEN
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.800
High resolution limit [Å]1.6901.700

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Rmerge0.0550.257
Total number of observations298712

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Number of reflections64713

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<I/σ(I)>36.163.3
Completeness [%]96.075

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Redundancy4.661.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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6.5

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Golubev, A. M., (1992) J. Mol. Biol., 226, 271.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10-15 (mg/ml)
21dropPEG600030 (%(w/v))
31dropsodium phosphate0.15 (M)
41reservoirPEG600030 (%(w/v))
51reservoirsodium phosphate0.15 (M)

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