1fts: Difference between revisions

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[[Image:1fts.jpg|left|200px]]<br /><applet load="1fts" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1fts.jpg|left|200px]]<br /><applet load="1fts" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1fts, resolution 2.2Å" />

'''SIGNAL RECOGNITION PARTICLE RECEPTOR FROM E. COLI'''<br />

==Overview==

FtsY is the docking protein or SR alpha homologue in E. coli. It is, involved in targeting secretory proteins to the cytoplasmic membrane by, interacting with the signal recognition particle, controlled by guanosine, 5'-triphosphate. Two different constructs have been used in, crystallization studies: the full-length protein and a truncated fragment, with a his-tag at the C terminus. Only the second construct resulted in, crystals suitable for x-ray diffraction. The crystals belong to the, monoclinic space group P2(1) with cell dimensions a = 32.20 A, b = 79.57, A, c = 59.21 A, and beta = 94.45, and contain one molecule per asymmetric, unit. At cryogenic temperatures the crystals diffract to a resolution, limit of 2.5 A by using a rotating anode, and beyond 1.8 A by using, synchrotron radiation.

FtsY is the docking protein or SR alpha homologue in E. coli. It is involved in targeting secretory proteins to the cytoplasmic membrane by interacting with the signal recognition particle, controlled by guanosine 5'-triphosphate. Two different constructs have been used in crystallization studies: the full-length protein and a truncated fragment with a his-tag at the C terminus. Only the second construct resulted in crystals suitable for x-ray diffraction. The crystals belong to the monoclinic space group P2(1) with cell dimensions a = 32.20 A, b = 79.57 A, c = 59.21 A, and beta = 94.45, and contain one molecule per asymmetric unit. At cryogenic temperatures the crystals diffract to a resolution limit of 2.5 A by using a rotating anode, and beyond 1.8 A by using synchrotron radiation.

==About this Structure==

1FTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FTS OCA].

1FTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FTS OCA].

==Reference==

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[[Category: signal recognition particle receptor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 15~~:16:~~35 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:40 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1fts.jpg|left|200px]]<br /><applet load="1fts" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fts.jpg|left|200px]]<br /><applet load="1fts" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fts, resolution 2.2&Aring;" />
 '''SIGNAL RECOGNITION PARTICLE RECEPTOR FROM E. COLI'''<br />
 ==Overview==
-FtsY is the docking protein or SR alpha homologue in E. coli. It is, involved in targeting secretory proteins to the cytoplasmic membrane by, interacting with the signal recognition particle, controlled by guanosine, 5'-triphosphate. Two different constructs have been used in, crystallization studies: the full-length protein and a truncated fragment, with a his-tag at the C terminus. Only the second construct resulted in, crystals suitable for x-ray diffraction. The crystals belong to the, monoclinic space group P2(1) with cell dimensions a = 32.20 A, b = 79.57, A, c = 59.21 A, and beta = 94.45, and contain one molecule per asymmetric, unit. At cryogenic temperatures the crystals diffract to a resolution, limit of 2.5 A by using a rotating anode, and beyond 1.8 A by using, synchrotron radiation.
+FtsY is the docking protein or SR alpha homologue in E. coli. It is involved in targeting secretory proteins to the cytoplasmic membrane by interacting with the signal recognition particle, controlled by guanosine 5'-triphosphate. Two different constructs have been used in crystallization studies: the full-length protein and a truncated fragment with a his-tag at the C terminus. Only the second construct resulted in crystals suitable for x-ray diffraction. The crystals belong to the monoclinic space group P2(1) with cell dimensions a = 32.20 A, b = 79.57 A, c = 59.21 A, and beta = 94.45, and contain one molecule per asymmetric unit. At cryogenic temperatures the crystals diffract to a resolution limit of 2.5 A by using a rotating anode, and beyond 1.8 A by using synchrotron radiation.
 ==About this Structure==
-FTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FTS OCA].
+FTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FTS OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: signal recognition particle receptor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:16:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:40 2008''