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1LQ2

Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with gluco-phenylimidazole

Experimental procedure
実験手法SINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsMACSCIENCE
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2001-08-15
DetectorRIGAKU RAXIS IV
Wavelength(s)1.5418
Spacegroup nameP 43 21 2
格子定数 [Å]100.693, 100.693, 182.676
格子定数 [度]90.00, 90.00, 90.00
精密化法
残基25.000 - 2.620

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Rwork0.210
R-free0.27290

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Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ieq
結合長の平均二乗偏差(RMSD) [Å]0.010
結合角の平均二乗偏差(RMSD) [度]1.700
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Quality characteristics
 OverallOuter shell
分解能 [Å] (低)50.0002.690
分解能 [Å] (高)2.6202.620
Rmerge_l_obs0.1300.583

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Total number of observations70377

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独立反射数44625

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<I/σ(I)>5.9
完全性 [%]73.6

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45.4

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冗長性1.81
結晶化条件
結晶ID方法pH温度溶液条件
1VAPOR DIFFUSION, HANGING DROP7277-279

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Hrmova, M., (1998) Acta Cryst., D54, 687.

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文献の結晶化試薬
ID結晶ID溶液試薬名濃度 (単位) (単位)詳細
11dropenzyme6.8 (mg/ml)
21dropHEPES-NaOH75 (mM)
31dropsodium acetate7.5 (mM)
41dropPEG4001.2 (%(w/v))
51dropammonium sulfate0.8 (M)
61reservoirammonium sulfate1.7 (M)
71reservoirHEPES-NaOH50 (mM)

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件を2024-09-18に公開中

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