2okh: Difference between revisions

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==Overview==

The crystals obtained from various batches of crystallization trials of, FabZ from Plasmodium falciparum exhibited non-isomorphism. The c axis of, the I222 cell showed a large variation of about 16 A, from c = 81 A to c =, 97 A. Complete data sets were collected for three crystal forms with, varying lengths of the c axis (form 1, c = 97 A; form 2, c = 92 A; form 3, c = 81 A). The crystal structure of form 1 has been reported previously., Here, the crystal structures of the other two crystal forms are reported, and a detailed structural comparison is made of the three crystal forms in, order to explore the possible reasons for the existence of, non-isomorphism. The conformations of three loops vary between the three, crystal forms. The disposition of the loops affects the crystal packing, and hence the unit-cell parameter. The crystallization condition and, crystallization method employed, which change the evaporation rate, determine the crystal form of the enzyme. The present analysis shows that, pH-induced intrinsic conformational changes in the protein play a key role, in the observed differences.

The crystals obtained from various batches of crystallization trials of FabZ from Plasmodium falciparum exhibited non-isomorphism. The c axis of the I222 cell showed a large variation of about 16 A, from c = 81 A to c = 97 A. Complete data sets were collected for three crystal forms with varying lengths of the c axis (form 1, c = 97 A; form 2, c = 92 A; form 3, c = 81 A). The crystal structure of form 1 has been reported previously. Here, the crystal structures of the other two crystal forms are reported and a detailed structural comparison is made of the three crystal forms in order to explore the possible reasons for the existence of non-isomorphism. The conformations of three loops vary between the three crystal forms. The disposition of the loops affects the crystal packing and hence the unit-cell parameter. The crystallization condition and crystallization method employed, which change the evaporation rate, determine the crystal form of the enzyme. The present analysis shows that pH-induced intrinsic conformational changes in the protein play a key role in the observed differences.

==About this Structure==

Line 14:

[[Category: Single protein]]

[[Category: Padala, P.]]

[[Category: Sharma, S.K.]]

[[Category: Sharma, S K.]]

[[Category: Suguna, K.]]

[[Category: Surolia, A.]]

[[Category: Surolia, N.]]

[[Category: Swarnamukhi, P.L.]]

[[Category: Swarnamukhi, P L.]]

[[Category: fabz]]

[[Category: hotdog fold]]

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[[Category: plasmodium]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystals obtained from various batches of crystallization trials of, FabZ from Plasmodium falciparum exhibited non-isomorphism. The c axis of, the I222 cell showed a large variation of about 16 A, from c = 81 A to c =, 97 A. Complete data sets were collected for three crystal forms with, varying lengths of the c axis (form 1, c = 97 A; form 2, c = 92 A; form 3, c = 81 A). The crystal structure of form 1 has been reported previously., Here, the crystal structures of the other two crystal forms are reported, and a detailed structural comparison is made of the three crystal forms in, order to explore the possible reasons for the existence of, non-isomorphism. The conformations of three loops vary between the three, crystal forms. The disposition of the loops affects the crystal packing, and hence the unit-cell parameter. The crystallization condition and, crystallization method employed, which change the evaporation rate, determine the crystal form of the enzyme. The present analysis shows that, pH-induced intrinsic conformational changes in the protein play a key role, in the observed differences.
+The crystals obtained from various batches of crystallization trials of FabZ from Plasmodium falciparum exhibited non-isomorphism. The c axis of the I222 cell showed a large variation of about 16 A, from c = 81 A to c = 97 A. Complete data sets were collected for three crystal forms with varying lengths of the c axis (form 1, c = 97 A; form 2, c = 92 A; form 3, c = 81 A). The crystal structure of form 1 has been reported previously. Here, the crystal structures of the other two crystal forms are reported and a detailed structural comparison is made of the three crystal forms in order to explore the possible reasons for the existence of non-isomorphism. The conformations of three loops vary between the three crystal forms. The disposition of the loops affects the crystal packing and hence the unit-cell parameter. The crystallization condition and crystallization method employed, which change the evaporation rate, determine the crystal form of the enzyme. The present analysis shows that pH-induced intrinsic conformational changes in the protein play a key role in the observed differences.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Padala, P.]]
-[[Category: Sharma, S.K.]]
+[[Category: Sharma, S K.]]
 [[Category: Suguna, K.]]
 [[Category: Surolia, A.]]
 [[Category: Surolia, N.]]
-[[Category: Swarnamukhi, P.L.]]
+[[Category: Swarnamukhi, P L.]]
 [[Category: fabz]]
 [[Category: hotdog fold]]
@@ Line 24: / Line 24: @@
 [[Category: plasmodium]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:12:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:28 2008''