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Three-dimensional structure of a new form of mare lactoferrin in <span style="font-size:14.0pt;font-family:"Times New Roman";mso-fareast-font-family: "Times New Roman";mso-ansi-language:EN-US;mso-fareast-language:EN-US; mso-bidi-language:AR-SA">70% PEG 400 at 3.8 Å resolution</span>

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Title Three-dimensional structure of a new form of mare lactoferrin in 70% PEG 400 at 3.8 Å resolution
 
Creator Kumar, S
Sharma, A K
Paramasivam, M
Srinivasan, A
Singh, T P
 
Description 135-141
Three-dimensional (3D) structure of a new form of
diferric mare lactoferrin has been determined at 3.8 Å resolution. The protein was crystallized in  space group P212121
with a=80.1 Å, b= 103.7 Å, c= 112.2 Å
with a solvent content of 57%. The structure was solved by molecular
replacement method using the model of native mare lactoferrin. The structure has
been refined

using X-PLOR to a final R-factor of 22.6% for all the
data in 15.0-3.8 Å resolution range. The final refined model comprises
5281 protein atoms, 2Fe3+ and 2CO32- ions. The protein folds into two globular N- and
C-Iobes. The two lobes are further divided into two domains N I, N2 in the
N-Iobe and C I, C2 in the C-Iobe. The overall folding of the protein

is similar to that observed for the native protein.
The superposition of Cα traces of native mare lactoferrin and the
present structure gives an r.m.s shift of 0.7 Å. There is a slight variation in the orientation of two
lobes but the domain orientations in the present structure are identical to
those observed in the native mare lactoferrin.
 
Date 2012-12-24T18:36:10Z
2012-12-24T18:36:10Z
2001-06
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15284
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.38(3) [June 2001]