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1GT7

L-rhamnulose-1-phosphate aldolase from Escherichia coli

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineX11
Temperature [K]100
Detector technologyIMAGE PLATE
DetectorMARRESEARCH
Spacegroup nameP 32 2 1
Unit cell lengths225.760, 225.760, 285.645
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution44.000 - 2.700
R-factor0.233

*

Rwork0.233
R-free0.23500
Structure solution methodSIR
Data scaling softwareSCALA
Phasing softwareSCALEIT
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]45.0002.770
High resolution limit [Å]2.7002.700
Rmerge0.0890.370

*

Total number of observations611276

*

Number of reflections207606
<I/σ(I)>7.82.1
Completeness [%]91.0

*

90

*

Redundancy2.92.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.6293

*

HANGING DROP CONTAINED 5 MG/ML PROTEIN, 5 MM PGH, 0.9 M SODIUM FORMATE, 5 MM MERCAPTOETHANOL, 0.5 MM ZNCL2 AND 0.1 M SODIUM ACETATE (PH 4.6). RESERVOIR CONTAINED 1.8 M SODIUM FORMATE, 5 MM MERCAPTOETHANOL AND 0.1 M SODIUM ACETATE (PH 4.6)
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein5 (mg/ml)
21dropphosphoglycolohydroxamate5 (mM)
31dropsodium formate0.9 (M)
41dropbeta-mercaptoethanol5 (mM)
51drop0.5 (mM)
61dropsodium acetate0.1 (M)pH4.6
71reservoirsodium formate1.8 (M)
81reservoirbeta-mercaptoethanol5 (mM)
91reservoirsodium acetate0.1 (M)pH4.6

219869

PDB entries from 2024-05-15

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