Crystallization and preliminary X-ray diffraction analysis of the regulatory subunit of human protein kinase CK2

1999 ◽  
Vol 55 (4) ◽  
pp. 895-897 ◽  
Author(s):  
Laurent Chantalat ◽  
Didier Leroy ◽  
Odile Filhol ◽  
Nora Quitaine ◽  
Edmond M. Chambaz ◽  
...  

Protein kinase CK2 is a tetramer composed of two α catalytic subunits and two β regulatory subunits. A C-terminal truncated form of the β subunit has been overproduced in Escherichia coli and purified to homogeneity. Two crystal forms of the truncated protein which diffract to at least 2 Å resolution have been obtained. Form I belongs to the monoclinic space group P21, with unit-cell parameters a = 49.9, b = 92.9, c = 53.7 Å, β = 96.3°, and yields plate-like crystals. Form II belongs to the tetragonal space group P42212, with unit-cell parameters a = 132.19, b = 132.19, c = 63.79 Å, and produces rod-shaped crystals. Both crystal forms have a functional dimer in the crystal asymmetric unit.

1998 ◽  
Vol 54 (1) ◽  
pp. 143-145 ◽  
Author(s):  
Barbara Guerra ◽  
Karsten Niefind ◽  
Lorenzo A. Pinna ◽  
Dietmar Schomburg ◽  
Olaf-Georg Issinger

The catalytic (α) subunit of protein kinase CK2 (CK2α) was originally cloned and overexpressed in the Escherichia coli strain pT7-7/BL21(DE3). The protein has been purified to homogeneity and crystallized. The crystals belong to the monoclinic space group C2, they have unit-cell parameters a = 142.6, b = 61.3, c = 45.6 Å, β = 103.3° and diffract X-rays to at least 2.0 Å resolution. The calculated crystal packing parameter is Vm = 2.47 Å3 Da−1 suggesting that one CK2α molecule is contained in the asymmetric unit and that the solvent content of the unit cell is 50%.


1999 ◽  
Vol 55 (4) ◽  
pp. 907-909 ◽  
Author(s):  
Jun Masuda ◽  
Tetsuya Yamaguchi ◽  
Takamasa Tobimatsu ◽  
Tetsuo Toraya ◽  
Kyoko Suto ◽  
...  

Two crystal forms of Klebsiella oxytoca diol dehydratase complexed with cyanocobalamin have been obtained and preliminary crystallographic experiments have been performed. The crystals belong to two different space groups, depending on the crystallization conditions. One crystal (form I) belongs to space group P212121 with unit-cell parameters a = 76.2, b = 122.3, c = 209.6 Å, and diffracts to 2.2 Å resolution using an X-ray beam from a synchrotron radiation source. The other crystal (form II) belongs to space group P21 with unit-cell parameters a = 75.4, b = 132.7, c = 298.8 Å, β = 91.9°, and diffracts to 3.0 Å resolution. For the purpose of structure determination, a heavy-atom derivative search was carried out and some mercuric derivatives were found to be promising. Structure analysis by the multiple isomorphous replacement method is now under way.


Author(s):  
San Hadži ◽  
Abel Garcia-Pino ◽  
Kenn Gerdes ◽  
Jurij Lah ◽  
Remy Loris

The HigA2 antitoxin and the HigBA2 toxin–antitoxin complex fromVibrio choleraewere crystallized in complex with their operator box. Screening of 22 different DNA duplexes led to two crystal forms of HigA2 complexes and one crystal form of a HigBA2 complex. Crystals of HigA2 in complex with a 17 bp DNA duplex belong to space groupP3221, with unit-cell parametersa=b= 94.0,c= 123.7 Å, and diffract to 2.3 Å resolution. The second form corresponding to HigA2 in complex with a 19 bp duplex belong to space groupP43212 and only diffract to 3.45 Å resolution. Crystals of the HigBA2 toxin–antitoxin were obtained in complex with a 31 bp duplex and belonged to space groupP41212, with unit-cell parametersa=b= 113.6,c= 121.1 Å. They diffract to 3.3 Å resolution.


1999 ◽  
Vol 55 (11) ◽  
pp. 1928-1929 ◽  
Author(s):  
Junichi Komoto ◽  
Yafei Huang ◽  
Yongbo Hu ◽  
Yoshimi Takata ◽  
Kiyoshi Konishi ◽  
...  

Guanidinoacetate methyltransferase is the enzyme which catalyzes the last step of creatine biosynthesis. The enzyme is found ubiquitously and in abundance in the livers of all vertebrates. Recombinant rat-liver guanidinoacetate methyltransferase has been crystallized with guanidinoacetate and S-adenosylhomocysteine. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 54.8, b = 162.5, c = 56.1 Å, β = 96.8 (1)° at 93 K, and typically diffract beyond 2.8 Å.


2020 ◽  
Vol 28 (2) ◽  
pp. 290-294
Author(s):  
Martin Števko ◽  
Jiří Sejkora ◽  
Zdeněk Dolníček

A new occurrence of pseudomalachite was recently discovered at the Zadné Breziny copper occurrence near Gemerská Poloma, Rožňava Co., Košice Region, Slovakia. It forms dark green rich coatings and crusts, which consist of individual hemispherical aggregates up to 7 mm in size. Pseudostalactites up to 6 mm in size were also rarely observed. Pseudomalachite occurs in fractures and cavities of the quartz gangue or in fractures of the wall rock. It is associated with malachite, cuprite and native copper. The refined unit-cell parameters (for the monoclinic space group P21/c) are a 4.4805(5) Å, b 5.7504(6) Å, c 17.045(2) Å, β 91.12(1)° and V 439.06(6) Å3. Except of dominant contents of Cu and P only minor amounts of Al (up to 0.04 apfu), Fe (up to 0.02 apfu), As (up to 0.07 apfu) and S (up to 0.01 apfu) were detected in studied samples of pseudomalachite from the Zadné Breziny occurrence.


Author(s):  
Analio Dugarte-Dugarte ◽  
Nahum Ramírez Pineda ◽  
Luis Nieves ◽  
José Antonio Henao ◽  
Graciela Díaz de Delgado ◽  
...  

Almost 50 years after the initial report, the crystal structure of Cu2GeSe3, a I2-IV-VI3 semiconductor, has been revised using modern single-crystal X-ray diffraction data. The structure of this material can be properly described in the monoclinic space group Cc (No. 9) with unit-cell parameters a = 6.7703 (4) Å, b = 11.8624 (5) Å, c = 6.7705 (4) Å, β = 108.512 (6)°, V = 515.62 (5) Å3, Z = 4, rather than in the orthorhombic space group Imm2 (No. 44) with unit-cell parameters a = 11.860 (3), b = 3.960 (1), c = 5.485 (2) Å, V = 257.61 Å3, Z = 2, as originally proposed [Parthé & Garín (1971). Monatsh. Chem. 102, 1197–1208]. Contrary to what was observed in the orthorhombic structure, the distortions of the tetrahedra in the monoclinic structure are consistent with the distortions expected from considerations derived from the bond valence model. A brief revision of the structures reported for the I2-IV-VI3 family of semiconducting compounds (I: Cu, Ag; IV: Si, Ge, Sn; and VI: S, Se, Te) is also presented.


2021 ◽  
Vol 29 (2) ◽  
pp. 189-196
Author(s):  
Martin Števko ◽  
Jiří Sejkora ◽  
Zdeněk Dolníček

An interesting occurrence of olivenite and cornwallite was recently discovered in cavities of quartz at the Podlipa copper deposit near Ľubietová, Slovakia. Olivenite occurs as olive to pale green sprays or radial aggregates consisting of individual acicular crystals up to 5 mm long. Its refined unit-cell parameters (for the monoclinic space group P21/n) are: a 8.6192(13) Å, b 8.2300(11) Å, c 5.9349(8) Å, α 90.055(12)° and V 420.99(7) Å3. Studied olivenite shows intense chemical zoning caused by strong variation of As and P contents. Most of the zones are corresponding to olivenite (with P content ranging between 0.02 to 0.39 apfu), but darker zones or domains of As-rich libethenite (with As content ranging between 0.18 to 0.24 apfu) were occasionally observed. Cornwallite forms dark green massive fillings between olivenite crystals or microcrystalline botryoidal crusts. The refined unit-cell parameters (for the monoclinic space group P21/c) of botryoidal cornwallite from the Podlipa deposit are: a 4.6112(2) Å, b 5.7698(3) Å, c 17.4167(11) Å, β 92.009(5)° and V 463.10(3) Å3. The two compositional types of cornwallite were distinguished. The first type is represented by relatively homogenous aggregates with only minor contents of P (from 0.04 to 0.22 apfu). The second type occurs as polycrystalline fillings with strong chemical zoning and has much more significant variation of As and P contents, representing solid-solution series between P-rich cornwallite (with 1.41 apfu of As and 0.59 apfu of P) and As-rich pseudomalachite (with 1.37 apfu of P and 0.63 apfu of As).


2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Akhmatkhodja N. Yunuskhodjayev ◽  
Shokhista F. Iskandarova ◽  
Vahobjon Kh. Sabirov

Abstract The crystal structure of a copper(II) complex of protonated sildenafil, CuCl3C22H31N6O4S⋅2H2O was studied by single crystal X-ray diffraction. The compound crystallizes in the monoclinic space group P21/n with the unit cell parameters a = 15.4292(2), b = 9.06735(12), c = 21.1752(2) Å, V = 2945.48(7) Å3, Z = 4. The Cu atom is coordinated by the sildenafil ligand via the N2 atom of the pyrazolopyrimidine ring and by three chloride anions. Sildenafil is protonated at the methylated N6 atom of the piperazine ring and it is cation ligand with a 1+ charge.


2014 ◽  
Vol 70 (10) ◽  
pp. 1389-1393 ◽  
Author(s):  
Mulu Y. Lubula ◽  
Amanda Poplawaski ◽  
Karen C. Glass

The bromodomain-PHD finger protein 1 (BRPF1) is an essential subunit of the monocytic leukemia zinc (MOZ) histone acetyltransferase (HAT) complex and is required for complex formation and enzymatic activation. BRPF1 contains a structurally conserved bromodomain, which recognizes specific acetyllysine residues on histone proteins. The MOZ HAT plays a direct role in hematopoiesis, and deregulation of its activity is linked to the development of acute myeloid leukemia. However, the molecular mechanism of histone-ligand recognition by the BRPF1 bromodomain is currently unknown. The 117-amino-acid BRPF1 bromodomain was overexpressed inEscherichia coliand purified to homogeneity. Crystallization experiments of the BRPF1 bromodomain in complex with its H4K12ac and H2AK5ac histone ligands yielded crystals that were suitable for high-resolution X-ray diffraction analysis. The BRPF1 bromodomain–H4K12ac crystals belonged to the tetragonal space groupP43212, with unit-cell parametersa= 75.1,b= 75.1,c= 86.3 Å, and diffracted to a resolution of 1.94 Å. The BRPF1 bromodomain–H2AK5ac crystals grew in the monoclinic space groupP21, with unit-cell parametersa= 60.9,b= 55.6,c= 82.1 Å, β = 93.6°, and diffracted to a resolution of 1.80 Å. Complete data sets were collected from both crystal forms using synchrotron radiation on beamline X29 at Brookhaven National Laboratory (BNL).


Author(s):  
Wentao Diao ◽  
Xue Yang ◽  
Hao Zhou

The protein 26S proteasome regulatory subunit p27 is one of the four chaperones that help in the assembly of the 19S regulatory particle (RP) of the 26S proteasome. In the present work, the N-terminus of p27 (residues 1–128) fromMus musculuswas cloned, expressed, purified and crystallized alone and in complex with the C-terminal ATPase domain of Rpt5 (residues 173–442). The crystals of p27(1–128)diffracted to 1.7 Å resolution and belonged to space groupP212121, with unit-cell parametersa= 26.79,b= 30.39,c= 145.06 Å. Resolution-dependent Matthews coefficient probability analysis suggested the presence of only one molecule per asymmetric unit, with 40.5% solvent content and aVMvalue of 2.02 Å3 Da−1. The crystal of the p27(1–128)–Rpt5(173–442)complex diffracted to 4 Å resolution and belonged to space groupP222, with unit-cell parametersa= 75.93,b= 76.08,c= 336.85 Å. The presence of four heterodimers in the asymmetric unit with 53.2% solvent content and aVMvalue of 2.63 Å3 Da−1or five heterodimers in the asymmetric unit with 41.5% solvent content and aVMvalue of 2.10 Å3 Da−1is assumed.


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