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PDBsum entry 1fu2

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protein metals Protein-protein interface(s) links
Hormone/growth factor PDB id
1fu2
Jmol
Contents
Protein chains
21 a.a.
30 a.a. *
Metals
_ZN ×4
_CL ×4
_NA ×2
* Residue conservation analysis
PDB id:
1fu2
Name: Hormone/growth factor
Title: First protein structure determined from x-ray powder diffrac
Structure: Insulin, a chain. Chain: a, c, e, g. Fragment: a chain of t3r3 variant. Engineered: yes. Insulin, b chain. Chain: b, d, f, h. Fragment: b chain of t3r3 variant. Engineered: yes
Source: Synthetic: yes. Other_details: this sequence occurs naturally in humans. Other_details: this sequence occurs naturally in humans
Biol. unit: Dodecamer (from PQS)
Authors: R.B.Von Dreele,P.W.Stephens,R.H.Blessing,G.D.Smith
Key ref:
R.B.Von Dreele et al. (2000). The first protein crystal structure determined from high-resolution X-ray powder diffraction data: a variant of T3R3 human insulin-zinc complex produced by grinding. Acta Crystallogr D Biol Crystallogr, 56, 1549-1553. PubMed id: 11092920 DOI: 10.1107/S0907444900013901
Date:
13-Sep-00     Release date:   16-Oct-00    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
21 a.a.
Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
30 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1107/S0907444900013901 Acta Crystallogr D Biol Crystallogr 56:1549-1553 (2000)
PubMed id: 11092920  
 
 
The first protein crystal structure determined from high-resolution X-ray powder diffraction data: a variant of T3R3 human insulin-zinc complex produced by grinding.
R.B.Von Dreele, P.W.Stephens, G.D.Smith, R.H.Blessing.
 
  ABSTRACT  
 
X-ray diffraction analysis of protein structure is often limited by the availability of suitable crystals. However, the absence of single crystals need not present an insurmountable obstacle in protein crystallography any more than it does in materials science, where powder diffraction techniques have developed to the point where complex oxide, zeolite and small organic molecular structures can often be solved from powder data alone. Here, that fact is demonstrated with the structure solution and refinement of a new variant of the T(3)R(3) Zn-human insulin complex produced by mechanical grinding of a polycrystalline sample. High-resolution synchrotron X-ray powder diffraction data were used to solve this crystal structure by molecular replacement adapted for Rietveld refinement. A complete Rietveld refinement of the 1630-atom protein was achieved by combining 7981 stereochemical restraints with a 4800-step (d(min) = 3.24 A) powder diffraction pattern and yielded the residuals R(wp) = 3.73%, R(p) = 2.84%, R(F)(2) = 8.25%. It was determined that the grinding-induced phase change is accompanied by 9.5 and 17.2 degrees rotations of the two T(3)R(3) complexes that comprise the crystal structure. The material reverts over 2-3 d to recover the original T(3)R(3) crystal structure. A Rietveld refinement of this 815-atom protein by combining 3886 stereochemical restraints with a 6000-step (d(min) = 3.06 A) powder diffraction pattern yielded the residuals R(wp) = 3.46%, R(p) = 2.64%, R(F)(2) = 7.10%. The demonstrated ability to solve and refine a protein crystal structure from powder diffraction data suggests that this approach can be employed, for example, to examine structural changes in a series of protein derivatives in which the structure of one member is known from a single-crystal study.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 (a) High-resolution X-ray powder diffraction pattern of freshly ground Zn-human insulin complex (T[3]R[3]DC) taken with = 0.700233 at 2 s step-1 and 0.002 step-1. (b) High-resolution X-ray powder diffraction pattern of aged Zn-human insulin complex (T[3]R[3]) taken with = 0.700233 ; the scan shown is sum of two scans taken at 2 s step-1 and 0.002 step-1.
Figure 3.
Figure 3 The relative orientations of the human insulin peptide backbones for TR dimers in the T[3]R[3] and T[3]R[3]DC hexamer structures. Two dimers stacked along the c axis are shown in green for T[3]R[3] and in red for T[3]R[3]DC. The two unit-cell origins are coincident near the center of the dimers at the bottom of the figure.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 1549-1553) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19462064 M.T.Weller, P.F.Henry, V.P.Ting, and C.C.Wilson (2009).
Crystallography of hydrogen-containing compounds: realizing the potential of neutron powder diffraction.
  Chem Commun (Camb), (), 2973-2989.  
18156682 I.Margiolaki, and J.P.Wright (2008).
Powder crystallography on macromolecules.
  Acta Crystallogr A, 64, 169-180.  
18611844 M.W.van der Kamp, K.E.Shaw, C.J.Woods, and A.J.Mulholland (2008).
Biomolecular simulation and modelling: status, progress and prospects.
  J R Soc Interface, 5, S173-S190.  
18156673 W.I.David, and K.Shankland (2008).
Structure determination from powder diffraction data.
  Acta Crystallogr A, 64, 52-64.  
15169448 J.C.Spence, and R.B.Doak (2004).
Single molecule diffraction.
  Phys Rev Lett, 92, 198102.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.