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6OR9

Structure of L-lactate dehydrogenase from Trichoplusia ni

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 21-ID-F
Synchrotron siteAPS
Beamline21-ID-F
Temperature [K]100
Detector technologyCCD
Collection date2018-11-29
DetectorRAYONIX MX-300
Wavelength(s)0.97872
Spacegroup nameP 1
Unit cell lengths63.390, 76.480, 79.520
Unit cell angles113.06, 109.84, 88.70
Refinement procedure
Resolution48.910 - 1.800
R-factor0.159
Rwork0.158
R-free0.19500
Structure solution methodSAD
RMSD bond length0.008
RMSD bond angle0.870
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwarePHASER
Refinement softwarePHENIX
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]48.9061.850
High resolution limit [Å]1.8001.800
Rmerge0.0390.344
Number of reflections115247
<I/σ(I)>17.552.74
Completeness [%]96.793.1
Redundancy2.9512.68
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.5290MCSG1 H11: 25% (W/V) PEG 3350, 200MM SODIUM CHLORIDE, 100MM HEPES FREE ACID / NAOH PH 7.5: TRNIA.00711.a.GL11.PS38300 AT 14.3 MG/ML + 2MM ATP: CRYO: 15% EG + BSI1767: TRAY 295240 H11: PUCK DAC0-8 FOR EXPERIMENTAL PHASING, A CRYSTAL FROM THE SAME DROP WAS INCUBATED FOR 15 SEC IN A SOLUTION OF 85% RESERVOIR AND 15% 2.5M SODIUM IODIDE IN ETHYLENE GLYCOL (FINAL IODIDE CONCENTRATION 375MM), AND VITRIFIED IN LIQUID NITROGEN: TRAY 295240H11: PUCK ANX5-15. THE PROTEIN WAS ACCIDENTALLY PURIFIED FROM A CULTURE THAT WAS SUPPOSED TO EXPRESS SSGCID PROTEIN PLFAA.18754.A.GL11., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
1VAPOR DIFFUSION, SITTING DROP7.5290MCSG1 H11: 25% (W/V) PEG 3350, 200MM SODIUM CHLORIDE, 100MM HEPES FREE ACID / NAOH PH 7.5: TRNIA.00711.a.GL11.PS38300 AT 14.3 MG/ML + 2MM ATP: CRYO: 15% EG + BSI1767: TRAY 295240 H11: PUCK DAC0-8 FOR EXPERIMENTAL PHASING, A CRYSTAL FROM THE SAME DROP WAS INCUBATED FOR 15 SEC IN A SOLUTION OF 85% RESERVOIR AND 15% 2.5M SODIUM IODIDE IN ETHYLENE GLYCOL (FINAL IODIDE CONCENTRATION 375MM), AND VITRIFIED IN LIQUID NITROGEN: TRAY 295240H11: PUCK ANX5-15. THE PROTEIN WAS ACCIDENTALLY PURIFIED FROM A CULTURE THAT WAS SUPPOSED TO EXPRESS SSGCID PROTEIN PLFAA.18754.A.GL11., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K

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