Sandbox Reserved 350: Difference between revisions

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Protein: cHuman Coagulation factor V, 1czv

:Protein: cHuman Coagulation factor V, 1czv <ref name="Pubmed">PMID: 10586886 </ref>

~~{{STRUCTURE_1czv|PDB|SCENE~~=}}

='''Introduction'''=

Coagulation Factor V originally studied in 1987 by William H. Kane, Akitada Ichinose, Frederick S. Hagen and Earl W. Davie, out of University of Washington, Seattle. <ref name="Old">PMID: 2827731 </ref>

[http://en.wikipedia.org/wiki/Coagulation_cascade Coagulation] is a complex cascade of a biological reaction that takes place after an injury causing bleeding, to prevent bleeding; A step of hemostatsis, which facilitates the formation of fibrin. There approximately 30 known factors which play a role in this massive cascade response. A possible explanation for the sheer complexity associated with what is known about this cascade is that tight regulation for the formation of blood clots are crucial.

The role of Human Coagulation Factor V is to act as a cofactor along with Factor X and Prothrombin (Factor II, inactive) to form a [http://en.wikipedia.org/wiki/Prothrombinase Prothrombinase] complex activating Prothrobin to Thrombin (FIIa). Thrombin is then able to activate Fibrinogen (Factor I) into Fibrin (FIa), which connects platelets bound at the site of injury; formation of a clot.

It is vital for controlled blood clot formation based on known human diseases/conditions of irregular clotting which are quiet devastating. Two clear aspects of blood clotting involve either under clotting or excessive clotting. The inability to form a clot leads to excessive bleeding from a minor abration known as [http://en.wikipedia.org/wiki/Haemophilia hemophila]. <ref name="Hemo">PMID: 21453683 </ref> [http://en.wikipedia.org/wiki/Thrombosis Thrombosis] is the second case, where excessive clotting or clotting when no wound is present results in free floating embolisms or thombuses. <ref name="Throm">PMID: 21455860 </ref> Floating free in the blood allows the thrombus to lodge itself within the circulatory system, interferring with orgran downstream of the circulating blood. Unusual blood circulation/clotting by a thrombus are causes of heart attacks, strokes and necrosis of tissue. <ref name="Throm2">PMID: 21359071 </ref>

__TOC__

=Structure & Function=

The structure of Human Coagulation Factor V (FV) precursors from a translated polypeptide

to a A1-A2-B-A3-C1-C2 layout which results in the activated (FVa) protein.<ref name="Pubmed"/>

*'''Heavy A1-A2 Chain'''

*'''Light A3-C1-C2 Chain'''

The '''C2 Domain''' of FVa (FVa-C2) consists of a conserved ''' β-Barrel framework ''' acting as a scaffold for '''three loops''' being part of the light chain. <ref name="Pubmed"/>

'''The FVa-C2''', which is classified as a ''' distorted jelly-roll ''' <scene name='Sandbox_Reserved_350/Expriment3/1'> β-barrel motif </scene>, is composed of <scene name='Sandbox_Reserved_350/Expriment5/1'> eight major antiparallel strands </scene> arranged into two ''' β-sheets of five and three strands ''' packed against one another.

Salt bridges located within the "upper" segment ''' (Asp61-Arg134) . The C2-Domain of Human coagulation factor is homologous to a larger family of adhesion proteins; [http://proteopedia.org/wiki/index.php/Category:Discoidin_family Discoidin], but not related to synaptotagmin-like C2 domains.<ref name="Pubmed"/>

<scene name='Sandbox_Reserved_350/Expriment2/4'> '''The Three Loops'''</scene> <ref name="Pubmed"/>

*'''Apex 1'''—'''Ser21-Trp31;''' containing Indole moieties able to form hydrogen bonds (Involving two consecutive Trp 26 & 27).

*'''Apex 2'''—'''Asn39-Asn45;''' capped with a basic residue able to form hydrogen bonds (Arg43).

*'''Apex 3'''—'''Gly75-Tyr84;''' Hydrophobic Loop (Leu79).

The apexes of these '''three loops''' within the C2 domain, are able to create a deep groove lined by '''hydrophobic''' '''(Trp31, Met83)''' and '''polar residues''' '''(Gln48, Ser78)''', as seen and consisting the <scene name='Sandbox_Reserved_350/Expriment3/3'> Open Form </scene> of FVa-C2. This groove is seen as the primary membrane-binding site of the C2-Domain. <ref name="Pubmed"/>

A second dimeric crystal form of FVa-C2, packed through the free edges of S6 strands, presenting a different Leu104-Val109

loop, suggests capabilities of adopting a "Closed Form". In contrast to the "Open Form" of FVa-C2; when looking at the loops 1 and 3 are tilted towards the interior of the groove. This change is considered due to a twist around '''Gly28''' cause it to be deformed (pseudo). In general there is a narrowing of the entrance to the shallow inner loop groove, particularly the critical Gln48 carboxamide; Taking place due form the concerted tilting/ "twisting" of the main chain atoms, shifting up to ~7Å and a 12Å displacement of the Trp27 moiety <big>→</big> shifting closer to the other two loops. Once shifted closer, the groove seen in the '''Open Form''' is covered by a hydrophobic ridge of Trp27, Trp27 and Leu79, and now in the '''Closed Form''' with a smaller, 370Å hydrophobic surface compared to 520Å. <ref name="Pubmed"/>

The three loops are described by ''Macedo-Ribeiro et al.'' to protrude like spikes from the bottom of the barrel in monomeric FVa-C2.<ref name="Pubmed"/> It is also worth noting that spike (1) & spike (3) are separated by β-hairpin structures and spike (2) is described as a wider irregularly loop comparatively. These three loops extending from the C2 domain, are all linked to each other, and to '''three shorter loops''' by an intricate '''H-bonding network''' which extends to residues at the bottom of the β-barrel.<ref name="Pubmed"/>

The overall Barrel structure is closed at the top and bottom by straight segments, giving it an overall spherical shape with a flattened upper surface.

Functionality of Human Coagulation Factor V (FV), as most proteins is strongly correlated to the conformation of the overall structure. As noted above in the structural section, two structural forms of Human Coagulation Factor V C2 Domain were crystallized. These two structures were distinct from each other based on a conformational change present, alternating between what was described as a Open and Closed form. This change from close to open by exposing this groove results due to the kind of environment Human Coagulation Factor V finds itself in, and ultimately the source of its function. This confers that FV is not an enzymatically active protein, but instead acts a cofactor part of the larger [http://en.wikipedia.org/wiki/File:Coagulation_full.svg Coagulation Cascade.]

The role of Human Coagulation Factor V, is act as a cofactor, enhances the ability of factor Xa to generate from prothrombin once activated (Fva). It is known that FV is activated in a positive feedback mechanism by α-thrombin and aided in conjunction with Human Coagulation Factor Xa, and inhibited by [http://en.wikipedia.org/wiki/Protein_C Active Protein C] [http://www.proteopedia.org/wiki/index.php/1aut (1aut)].

Originally, the activation of FV to Fva was understood to require the excision of B segment between the heavy and light chain at Arg-1018 and Arg-1545. The peptide as a whole remains united via the disulfide linkage connecting the N and C Terminus and interactions with calcium ions. <ref name="Old"/> In 1999, the [[#Finer Crystallography Details| crystallization]] of FV in both Fv and Fva was identified providing further insight into the quaternary structure of FV and the underlining mechanism by which the protein functions. <ref name="Pubmed"/> This mechanism proposed has three novel points, which were over-looked based on assumed knowledge from previous studies modeling the mechanism for FV after the well characterized mechanism of vitamin K-dependent [http://en.wikipedia.org/wiki/Coagulation Coagulation Factors]; [http://en.wikipedia.org/wiki/Factor_VII VII] [http://proteopedia.org/wiki/index.php/1dan (1dan)]

, [http://en.wikipedia.org/wiki/Factor_IX IX] [http://proteopedia.org/wiki/index.php/1pfx (1pfx)]

, [http://en.wikipedia.org/wiki/Factor_X X] [http://proteopedia.org/wiki/index.php/1c5m (1c5m)]

and Protein C <ref name="KA">PMID: 10200912</ref>

The '''Mechanism Proposed''' <ref name="Pubmed"/> differs from the previous work, showing Ca2+-Independent stereospecific binding to phospholipid membranes, based on;

'''(1)''' Immersion of Hydrophobic residues at the apices of loops in apolar membrane core.

'''(2)''' Specific Interactions with phosphatidylserine head groups in the groove enclosed by these loops.

'''(3)''' Favourable electrostatic contacts of basic side chains with negatively charged membrane phosphate groups.

==Detailed Proposed Mechanism <ref name="Pubmed"/> ==

For stereospecific and cooperative association with (PʟS)-rich membranes.

'''(1)''' FVa, with C2 domain in its closed form, approaches acidic membranes directed by protein-membrane electrostatic interactions.

'''(2)''' One or two (PʟS) molecules bind to anchoring points Arg150 or Gln48 in small groove of closed from → triggers widening of the groove and conversion to the open form.

'''(3)''' [(Fig. 5a.)]–A (PʟS) molecule occupies the opened specificity pocket.

'''(4)''' Now the unfolded hydrophobic spikes, perforate the polar membrane surface; Trp26, Trp27 and Leu79 side are immersed into the apolar core.

'''(5)''' Bottom of β-Barrel contacts negatively charged phosphate head groups on the membrane through favourable ionic interactions with basic residues located in the spikes and neighboring loops. <ref name="Lipid-protein blood interaction ">PMID: 9805008 </ref> <ref name="Prothrobins and lipids ">PMID: 2261453 </ref>

:The C2 domain of FVa is essential for binding to phosphatidyl-ʟ-serine (PʟS). This is because the spikes and neighboring loops are highly connected and several continuous PʟS molecules would be necessary for association with spike unfolding and membrane insertion for a cooperative mechanism. This assures FVa-C2 binds only to cell membranes with the concentration of PʟS exceeding a critical threshold level and therefore selectively target FVa to procoagulated, PʟS-rich surfaces.

===Experimental Evidence ===

Binding of FVa to a few acidic, lipid-specific sites results in substantial protein conformational changes. <ref name="Pubmed"/>

*A3 Domain interacts with phosphatidyl-choline. <ref name="FVa and Light chain cofactor ">PMID: 8286378 </ref>

*Contributions from hydrophobicity of the heavy chains; A1 and A2. <ref name="Role of Heavy Chains in FVa ">PMID: 9370458 </ref>

*Speculation of further conformational changes as associated with membrane, where the C2 Domain rotates to bring spike 1 and the Trp-rich surface (flat and extended) covering the front-side of the β-Barrel in contact with the phospholipid membrane [(Fig. 5b.)]. <ref name="Pubmed"/>

=Finer Crystallography Details=

''[http://www.rcsb.org/pdb/explore/materialsAndMethods.do?structureId=1CZV X-Ray Diffraction of the C2 Domain of Human Coagulation Factor V] (1czv)'' <ref name="Pubmed"/>

'''Resolution Method:'''Structure Replacement

'''Resolution:''' 2.40Å

: ''High:'' 2.40Å

: ''Low:'' 8.00Å

'''Condition;'''

::''pH:'' 10.00

::''Temperature:'' 289.0K

::''Number of Crystals used:'' 1

'''Geometry:''' ''Unit Cell Length'' : ''Angle''

:::a= 86.52Å : α= 90°

:::b= 70.54Å : β= 90°

:::c= 60.58Å : γ= 90°

'''Radiation Source:''' Rotating Anode

'''Wavelength OR Range:''' 1.5418Å

'''Detector Type:''' Image Plate

=References=

Sandbox Reserved 350: Difference between revisions

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@@ Line 1: / Line 1: @@
- <!-- PLEASE DO NOT DELETE THIS TEMPLATE -->
+<!-- PLEASE DO NOT DELETE THIS TEMPLATE -->
 {{Template:Sandbox_Reserved_BCMB307}}
   <!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
-Protein: cHuman Coagulation factor V, 1czv
+:Protein: cHuman Coagulation factor V, 1czv <ref name="Pubmed">PMID: 10586886 </ref>
-{{STRUCTURE_1czv|PDB|SCENE=}}
+='''Introduction'''=
+<br />
+Coagulation Factor V originally studied in 1987 by William H. Kane, Akitada Ichinose, Frederick S. Hagen and Earl W. Davie, out of University of Washington, Seattle. <ref name="Old">PMID: 2827731 </ref>
+[http://en.wikipedia.org/wiki/Coagulation_cascade Coagulation] is a complex cascade of a biological reaction that takes place after an injury causing bleeding, to prevent bleeding; A step of hemostatsis, which facilitates the formation of fibrin.  There approximately 30 known factors which play a role in this massive cascade response.  A possible explanation for the sheer complexity associated with what is known about this cascade is that tight regulation for the formation of blood clots are crucial.
+<br />
+The role of Human Coagulation Factor V is to act as a cofactor along with Factor X and Prothrombin (Factor II, inactive) to form a [http://en.wikipedia.org/wiki/Prothrombinase Prothrombinase] complex activating Prothrobin to Thrombin (FIIa).  Thrombin is then able to activate Fibrinogen (Factor I) into Fibrin (FIa), which connects platelets bound at the site of injury; formation of a clot.
+<br />
+It is vital for controlled blood clot formation based on known human diseases/conditions of irregular clotting which are quiet devastating.  Two clear aspects of blood clotting involve either under clotting or excessive clotting.  The inability to form a clot leads to excessive bleeding from a minor abration known as [http://en.wikipedia.org/wiki/Haemophilia hemophila]. <ref name="Hemo">PMID: 21453683 </ref> [http://en.wikipedia.org/wiki/Thrombosis Thrombosis] is the second case, where excessive clotting or clotting when no wound is present results in free floating embolisms or thombuses. <ref name="Throm">PMID: 21455860 </ref> Floating free in the blood allows the thrombus to lodge itself within the circulatory system, interferring with orgran downstream of the circulating blood.  Unusual blood circulation/clotting by a thrombus are causes of heart attacks, strokes and necrosis of tissue. <ref name="Throm2">PMID: 21359071 </ref>
+{{STRUCTURE_1czv|PDB=1czv|SCENE=}}
-<Structure load='1czv'size='500' frame='true' align='right' caption='This is what i'm showing you' scene='Insert optional scene name here' />
+__TOC__
+=Structure & Function=
+The structure of Human Coagulation Factor V (FV) precursors from a translated polypeptide
+<br /> to a A1-A2-B-A3-C1-C2 layout which results in the activated (FVa) protein.<ref name="Pubmed"/>
+<br />
+*'''Heavy A1-A2 Chain'''
+*'''Light A3-C1-C2 Chain'''
+The '''C2 Domain''' of FVa (FVa-C2) consists of a conserved '''<font color='red'> β-Barrel  framework </font> ''' acting as a scaffold for <font color='orangered'> '''three loops''' </font> being part of the light chain. <ref name="Pubmed"/>
+<br />
+[[Image:3D Jellow B-Barrel Motif.png|thumb|left|upright=1.5|alt=Distorted Jelly-Roll β-barrel motif with three active loops. The β-barrel motif is labeled in red and the three loops in orange.|Secondary structure of C2 Domain of 1czv.]]
+<br />
+'''The FVa-C2''', which is classified as a ''' <font color='red'> distorted jelly-roll </font> ''' <scene name='Sandbox_Reserved_350/Expriment3/1'> β-barrel motif </scene>, is composed of <scene name='Sandbox_Reserved_350/Expriment5/1'> eight major antiparallel strands  </scene> arranged into two ''' <font color='lawngreen'> β-sheets of five </font> and <font color='maroon'> three strands </font> ''' packed against one another.
+<br />
+Salt bridges located within the "upper" segment ''' <font color='goldenrod'> (Asp61-Arg134) </font>.  The C2-Domain of Human coagulation factor is homologous to a larger family of adhesion proteins; [http://proteopedia.org/wiki/index.php/Category:Discoidin_family Discoidin], but not related to synaptotagmin-like C2 domains.<ref name="Pubmed"/>
+<br />
+<br />
+<br />
+<br />
+<br />
+<br />
+<br />
+<scene name='Sandbox_Reserved_350/Expriment2/4'> '''The Three Loops'''</scene>  <ref name="Pubmed"/>
+<br />
+*'''Apex 1'''—<font color='purple'>'''Ser21-Trp31;''' containing Indole moieties able to form hydrogen bonds (Involving two consecutive Trp 26 & 27). </font>
+*'''Apex 2'''—<font color='lightseagreen'>'''Asn39-Asn45;''' capped with a basic residue able to form hydrogen bonds (Arg43). </font>
+*'''Apex 3'''—<font color='deeppink'>'''Gly75-Tyr84;''' Hydrophobic Loop (Leu79). </font>
+<Structure load='1czv' size='' frame='true' align='right' caption=' C2 Domain of Human Coagulation Factor V' scene='Sandbox_Reserved_350/Expriment3/2'/>
+The apexes of these <font color='orangered'> '''three loops''' </font> within the C2 domain, are able to create a deep groove lined by '''hydrophobic''' <font color='brown'> '''(Trp31, Met83)''' </font> and '''polar residues''' <font color='royalblue'> '''(Gln48, Ser78)'''</font>, as seen and consisting the <scene name='Sandbox_Reserved_350/Expriment3/3'> Open Form </scene> of FVa-C2.  This groove is seen as the primary membrane-binding site of the C2-Domain. <ref name="Pubmed"/>
+<br />
+A second dimeric crystal form of FVa-C2, packed through the free edges of S6 strands, presenting a different Leu104-Val109
+loop, suggests capabilities of adopting a "Closed Form".  In contrast to the "Open Form" of FVa-C2; when looking at the loops 1 and 3 are tilted towards the interior of the groove.  This change is considered due to a twist around '''Gly28''' cause it to be deformed (pseudo).  In general there is a narrowing of the entrance to the shallow inner loop groove, particularly the critical Gln48 carboxamide; Taking place due form the concerted tilting/ "twisting" of the main chain atoms, shifting up to ~7Å and a 12Å displacement of the Trp27 moiety <big>&rarr;</big> shifting closer to the other two loops.  Once shifted closer, the groove seen in the '''Open Form''' is covered by a hydrophobic ridge of Trp27, Trp27 and Leu79, and now in the '''Closed Form''' with a smaller, 370Å hydrophobic surface compared to 520Å. <ref name="Pubmed"/>
+<br />
+The three loops are described by ''Macedo-Ribeiro et al.'' to protrude like spikes from the bottom of the barrel in monomeric FVa-C2.<ref name="Pubmed"/>  It is also worth noting that spike (1) & spike (3) are separated by β-hairpin structures and spike (2) is described as a wider irregularly loop comparatively.  These three loops extending from the C2 domain, are all linked to each other, and to '''three shorter loops''' by an intricate '''H-bonding network''' which extends to residues at the bottom of the β-barrel.<ref name="Pubmed"/>
+<br />
+The overall Barrel structure is closed at the top and bottom by straight segments, giving it an overall spherical shape with a flattened upper surface.
+<br />
+Functionality of Human Coagulation Factor V (FV), as most proteins is strongly correlated to the conformation of the overall structure.  As noted above in the structural section, two structural forms of Human Coagulation Factor V C2 Domain were crystallized.  These two structures were distinct from each other based on a conformational change present, alternating between what was described as a Open and Closed form.  This change from close to open by exposing this groove results due to the kind of environment Human Coagulation Factor V finds itself in, and ultimately the source of its function.  This confers that FV is not an enzymatically active protein, but instead acts a cofactor part of the larger [http://en.wikipedia.org/wiki/File:Coagulation_full.svg Coagulation Cascade.]
+<br />
+The role of Human Coagulation Factor V, is act as a cofactor, enhances the ability of factor Xa to generate  from prothrombin once activated (Fva).  It is known that FV is activated in a positive feedback mechanism by α-thrombin and aided in conjunction with Human Coagulation Factor Xa, and inhibited by [http://en.wikipedia.org/wiki/Protein_C Active Protein C] [http://www.proteopedia.org/wiki/index.php/1aut (1aut)].
+Originally, the activation of FV to Fva was understood to require the excision of B segment between the heavy and light chain at Arg-1018 and Arg-1545.  The peptide as a whole remains united via the disulfide linkage connecting the N and C Terminus and interactions with calcium ions. <ref name="Old"/>  In 1999, the [[#Finer Crystallography Details| crystallization]] of FV in both Fv and Fva was identified providing further insight into the quaternary structure of FV and the underlining mechanism by which the protein functions. <ref name="Pubmed"/>  This mechanism proposed has three novel points, which were over-looked based on assumed knowledge from previous studies modeling the mechanism for FV after the well characterized mechanism of vitamin K-dependent [http://en.wikipedia.org/wiki/Coagulation Coagulation Factors]; [http://en.wikipedia.org/wiki/Factor_VII VII] [http://proteopedia.org/wiki/index.php/1dan (1dan)]
+, [http://en.wikipedia.org/wiki/Factor_IX IX] [http://proteopedia.org/wiki/index.php/1pfx (1pfx)]
+, [http://en.wikipedia.org/wiki/Factor_X X] [http://proteopedia.org/wiki/index.php/1c5m (1c5m)]
+and Protein C <ref name="KA">PMID: 10200912</ref>
+<ref name="KB">PMID: 9805008 </ref>
+<br />
+<br />
+The '''Mechanism Proposed''' <ref name="Pubmed"/> differs from the previous work, showing Ca<sup>2+</sup>-Independent stereospecific binding to phospholipid membranes, based on;
+<br />
+'''(1)'''  Immersion of Hydrophobic residues at the apices of loops in apolar membrane core.
+<br />
+'''(2)'''  Specific Interactions with phosphatidylserine head groups in the groove enclosed by these loops.
+<br />
+'''(3)'''  Favourable electrostatic contacts of basic side chains with negatively charged membrane phosphate groups.
+<br />
+<br />
+<br />
+==Detailed Proposed Mechanism <ref name="Pubmed"/> ==
+For stereospecific and cooperative association with (P<sub>ʟ</sub>S)-rich membranes.
+<br />
+'''(1)'''  FVa, with C2 domain in its closed form, approaches acidic membranes directed by protein-membrane electrostatic interactions.
+<br />
+'''(2)'''  One or two (P<sub>ʟ</sub>S) molecules bind to anchoring points Arg150 or Gln48 in small groove of closed from → triggers widening of the groove and conversion to the open form.
+<br />
+'''(3)''' [(Fig. 5a.)]–A (P<sub>ʟ</sub>S) molecule occupies the opened specificity pocket.
+<br />
+'''(4)''' Now the unfolded hydrophobic spikes, perforate the polar membrane surface; Trp26, Trp27 and Leu79 side are immersed into the apolar core.
+<br />
+'''(5)''' Bottom of β-Barrel contacts negatively charged phosphate head groups on the membrane through favourable ionic interactions with basic residues located in the spikes and neighboring loops. <ref name="Lipid-protein blood interaction ">PMID: 9805008 </ref> <ref name="Prothrobins and lipids ">PMID: 2261453 </ref>
+<br />
+<br />
+:The C2 domain of FVa is essential for binding to phosphatidyl-ʟ-serine (P<sub>ʟ</sub>S).  This is because the spikes and neighboring loops are highly connected and several continuous P<sub>ʟ</sub>S molecules would be necessary for association with spike unfolding and membrane insertion for a cooperative mechanism.  This assures FVa-C2 binds only to cell membranes with the concentration of P<sub>ʟ</sub>S exceeding a critical threshold level and therefore selectively target FVa to procoagulated, P<sub>ʟ</sub>S-rich surfaces.
+<br />
+<br />
+===Experimental Evidence  ===
+Binding of FVa to a few acidic, lipid-specific sites results in substantial protein conformational changes. <ref name="Pubmed"/>
+<br />
+*A3 Domain interacts with phosphatidyl-choline. <ref name="FVa and Light chain cofactor ">PMID: 8286378 </ref>
+*Contributions from hydrophobicity of the heavy chains; A1 and A2. <ref name="Role of Heavy Chains in FVa ">PMID: 9370458 </ref>
+*Speculation of further conformational changes as associated with membrane, where the C2 Domain rotates to bring spike 1 and the Trp-rich surface (flat and extended) covering the front-side of the β-Barrel in contact with the phospholipid membrane [(Fig. 5b.)]. <ref name="Pubmed"/>
+<br />
+<br />
+<br />
+<br />
+=Finer Crystallography Details=
+''[http://www.rcsb.org/pdb/explore/materialsAndMethods.do?structureId=1CZV X-Ray Diffraction of the C2 Domain of Human Coagulation Factor V] (1czv)'' <ref name="Pubmed"/>
+<br />
+'''Resolution Method:'''Structure Replacement
+<br />
+'''Resolution:''' 2.40Å
+<br />
+: ''High:'' 2.40Å
+: ''Low:''  8.00Å
+<br />
+'''Condition;'''
+<br />
+::''pH:'' 10.00
+::''Temperature:'' 289.0K
+::''Number of Crystals used:'' 1
+<br />
+'''Geometry:''' ''Unit Cell Length''         :           ''Angle''
+<br />
+:::a= 86.52Å                    :            α= 90°
+:::b= 70.54Å                    :            β= 90°
+:::c= 60.58Å                    :            γ= 90°
+<br />
+'''Radiation Source:''' Rotating Anode
+<br />
+'''Wavelength OR Range:''' 1.5418Å
+<br />
+'''Detector Type:''' Image Plate
+=References=
+<references/>