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1BGA

BETA-GLUCOSIDASE A FROM BACILLUS POLYMYXA

Experimental procedure
Source typeSYNCHROTRON
Source detailsLURE
Synchrotron siteLURE
Temperature [K]176
Detector technologyIMAGE PLATE
Collection date1996-10
DetectorMARRESEARCH
Spacegroup nameP 42 21 2
Unit cell lengths205.460, 205.460, 155.860
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 2.400
R-factor0.2
Rwork0.200
R-free0.27000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1cbg
RMSD bond length0.009
RMSD bond angle24.000

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((AGROVATA)
Phasing softwareX-PLOR (3.843)
Refinement softwareX-PLOR (3.843)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]26.5402.460
High resolution limit [Å]2.4002.400
Rmerge0.083

*

0.300
Total number of observations584536

*

Number of reflections117344
<I/σ(I)>8.31.8
Completeness [%]97.392.3
Redundancy4.72.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1co-crystallization

*

8.3PROTEIN WAS CRYSTALLIZED FROM 1.3 M NA/K PHOSPHATE, PH 8.3, 5 MICRO-L PROTEIN, 14 MG/ML, 5 MICRO-L RESERVOIR
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropphosphate1.3 (M)
21dropinhibitor

223532

PDB entries from 2024-08-07

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