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2MEG

CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS.

Experimental procedure
Source typeSYNCHROTRON
Source detailsPHOTON FACTORY BEAMLINE BL-18B
Synchrotron sitePhoton Factory
BeamlineBL-18B
Temperature [K]283
Detector technologyIMAGE PLATE
Collection date1996-12-12
Spacegroup nameP 21 21 21
格子定数 [Å]57.100, 61.060, 33.760
格子定数 [度]90.00, 90.00, 90.00
精密化法
残基8.000 - 1.800
R因子0.151
Rwork0.151
Structure solution methodISOMORPHOUS METHOD
Starting model (for MR)WILD-TYPE OF HUMAN LYSOZYME
結合長の平均二乗偏差(RMSD) [Å]0.008
結合角の平均二乗偏差(RMSD) [度]23.900

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Quality characteristics
 OverallOuter shell
分解能 [Å] (低)1.830
分解能 [Å] (高)1.8001.800
Rmerge_l_obs0.0520.180
Total number of observations42094

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独立反射数10582

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<I/σ(I)>8.8
完全性 [%]92.280.9
冗長性2.5
結晶化条件
結晶ID方法pH温度溶液条件
1Vapor diffusion, hanging drop

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4.510

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Takano, K., (1995) J.Mol.Biol., 254, 62.

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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
11dropprotein10 (mg/ml)
21reservoir2.5 (M)
31reservoiracetate20 (mM)

218500

件を2024-04-17に公開中

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