Sharma, S. ; Singh, T. P. ; Bhatia, K. L. (1997) Crystallization and preliminary X-ray diffraction studies of the proteolytically engineered C-terminal half of buffalo lactoferrin in its iron-saturated form Acta Crystallographica Section D, D53 (1). pp. 116-118. ISSN 0907-4449
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Official URL: http://scripts.iucr.org/cgi-bin/paper?gr0654
Related URL: http://dx.doi.org/10.1107/S0907444996010591
Abstract
The glycosylated functional monoferric C-terminal half (C lobe) (Mr≃40 kDa) of buffalo lactoferrin has been produced by limited proteolysis using proteinase K. The iron-saturated C lobe has been crystallized by microdialysis. The crystals belong to the monoclinic system, space group P21 with unit-cell dimensions of a = 44.4, b = 152.3, c= 38.8 Åand = 105.5°. There is one protein molecule of 40 kDa in the asymmetric unit. A data set at 2.8 Åhas been collected on an imaging-plate scanner.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to International Union of Crystallography. |
| ID Code: | 49147 |
| Deposited On: | 19 Jul 2011 04:15 |
| Last Modified: | 19 Jul 2011 04:15 |
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