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1UA3

Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]298
Detector technologyIMAGE PLATE
Collection date1996-04-20
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameP 21 21 21
Unit cell lengths69.781, 113.183, 116.924
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution35.000

*

- 2.010
R-factor0.1835
Rwork0.175
R-free0.19800

*

Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.007

*

RMSD bond angle1.400

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]35.000

*

2.040
High resolution limit [Å]2.0102.010
Rmerge0.0550.218
Total number of observations211556

*

Number of reflections61415

*

<I/σ(I)>9.51.6
Completeness [%]98.385.8
Redundancy3.73.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

6.8

*

4

*

White, J.L., (1982) FEBS Lett., 148, 87.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropenzyme5 (mg/ml)
21droppotassium phosphate50 (mM)
31dropEDTA5 (mM)
41dropDTE1-2 (mM)
51dropPEG1000016-18 (%(w/v))
61reservoirPEG1000032-36 (%(w/v))

226707

PDB entries from 2024-10-30

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