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3ONW

Structure of a G-alpha-i1 mutant with enhanced affinity for the RGS14 GoLoco motif.

Experimental procedure
実験手法SINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 22-BM
Synchrotron siteAPS
Beamline22-BM
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2009-11-30
DetectorMAR scanner 300 mm plate
Wavelength(s)1.000
Spacegroup nameP 2 2 21
格子定数 [Å]70.392, 83.679, 190.148
格子定数 [度]90.00, 90.00, 90.00
精密化法
残基95.070 - 2.380
R因子0.22953
Rwork0.228
R-free0.26539
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2OM2 chain A
結合長の平均二乗偏差(RMSD) [Å]0.009
結合角の平均二乗偏差(RMSD) [度]1.086
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwarePHASER
Refinement softwareREFMAC (5.5.0109)
Quality characteristics
 OverallOuter shell
分解能 [Å] (低)28.8802.400
分解能 [Å] (高)2.3802.380
Rmerge_l_obs0.0650.761
独立反射数45328
<I/σ(I)>27.32.2
完全性 [%]98.8100
冗長性66
結晶化条件
結晶ID方法pH温度溶液条件
1VAPOR DIFFUSION, HANGING DROP5291Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (10 mM Tris pH 7.5, 1 mM magnesium chloride, 5% (w/v) glycerol, 5 mM DTT) and well solution (1.9 M ammonium sulfate, 100 mM sodium acetate pH 5.0, 200 mM magnesium chloride, 10% (w/v) glycerol), VAPOR DIFFUSION, HANGING DROP, temperature 291K

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件を2024-09-18に公開中

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