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1H54

Maltose phosphorylase from Lactobacillus brevis

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsLURE BEAMLINE D41A
Synchrotron siteLURE
BeamlineD41A
Temperature [K]100
Detector technologyIMAGE PLATE
DetectorMARRESEARCH
Spacegroup nameP 1 21 1
Unit cell lengths83.750, 102.500, 114.000
Unit cell angles90.00, 111.30, 90.00
Refinement procedure
Resolution29.100 - 2.150
R-factor0.173

*

Rwork0.186
R-free0.21400

*

Structure solution methodMIR
RMSD bond length0.005
RMSD bond angle23.700

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.350
High resolution limit [Å]2.1502.150
Rmerge0.076

*

Number of reflections95868
<I/σ(I)>237.7
Completeness [%]98.295.7
Redundancy3.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

6O.1 M CITRATE, 0.03M PHOSPHATE; PH 6.0, 20% POLY ACRYLIC ACID 20000
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein8-10 (mg/ml)
21dropcitrate10 (mM)
31reservoirPAA2000018 (%)
41reservoircitrate0.1 (M)
51reservoirphosphate0.03 (M)

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PDB entries from 2024-09-18

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