Mass: 18.015 Da / Num. of mol.: 234 / Source method: isolated from a natural source / Formula: H2O
Sequence details
N-TERMINAL SEGMENT GPLGSPEFG ARE CARRIED OVER FROM THE EXPRESSION VECTOR AFTER PROTEASE CLEAVAGE
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 2.18 Å3/Da / Density % sol: 43.68 % / Description: NONE
Crystal grow
Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 10% PEG 5000 MONOMETHYL ETHER, 0.1 M BIS-TRIS PH 6.5 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K.
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Data collection
Diffraction
ID
Mean temperature (K)
Crystal-ID
1
95
1
2
1
Diffraction source
Source
Site
Beamline
Type
ID
Wavelength
ROTATING ANODE
RIGAKU RU200
1
1.5418
SYNCHROTRON
APS
22-ID
2
1.2818
Detector
Type
ID
Detector
Date
Details
RIGAKU-MSC
1
IMAGE PLATE
Mar 6, 2006
MIRRORS
MARRESEARCH
2
CCD
Radiation
ID
Protocol
Monochromatic (M) / Laue (L)
Scattering type
Wavelength-ID
1
SINGLEWAVELENGTH
M
x-ray
1
2
SINGLEWAVELENGTH
M
x-ray
1
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
1.5418
1
2
1.2818
1
Reflection
Resolution: 2.4→30 Å / Num. obs: 11048 / % possible obs: 99.4 % / Observed criterion σ(I): 1.8 / Redundancy: 3.3 % / Biso Wilson estimate: 30.5 Å2 / Rmerge(I) obs: 0.15 / Net I/σ(I): 8.1
Reflection shell
Resolution: 2.4→2.49 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 1.8 / % possible all: 95.7
-
Processing
Software
Name
Version
Classification
CNS
1.1
refinement
HKL-2000
datareduction
HKL-2000
datascaling
PHASER
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: PROTEIN MODEL DETERMINED BY SAD Resolution: 2.4→30 Å / Rfactor Rfree error: 0.01 / Cross valid method: THROUGHOUT / σ(F): 1.8
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