Structure of a monoclinic polymorph of human carbonic anhydrase II with a doubled a axis
The crystal structure of human carbonic anhydrase II with a doubled a axis from that of the usually observed monoclinic unit cell has been determined and refined to 1.4 Å resolution. The diffraction data with h = 2n + 1 were systematically weaker than those with h = 2n. Consequently, the scaling of...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2010-05, Vol.66 (5), p.628-634 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
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| creator | Robbins, Arthur H. Domsic, John F. Agbandje-McKenna, Mavis McKenna, Robert |
| description | The crystal structure of human carbonic anhydrase II with a doubled a axis from that of the usually observed monoclinic unit cell has been determined and refined to 1.4 Å resolution. The diffraction data with h = 2n + 1 were systematically weaker than those with h = 2n. Consequently, the scaling of the data, structure solution and refinement were challenging. The two molecules comprising the asymmetric unit are related by a noncrystallographic translation of ½ along a, but one of the molecules has two alternate positions related by a rotation of approximately 2°. This rotation axis is located near the edge of the central β‐sheet, causing a maximum distance disparity of 1.7 Å between equivalent atoms on the diametrically opposite side of the molecule. The crystal‐packing contacts are similar to two sequential combined unit cells along a of the previously determined monoclinic unit cell. Abnormally high final Rcryst and Rfree values (20.2% and 23.7%, respectively) are not unusual for structures containing pseudo‐translational symmetry and probably result from poor signal to noise in the weak h‐odd data. |
| doi_str_mv | 10.1107/S0907444910006797 |
| format | Article |
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The diffraction data with h = 2n + 1 were systematically weaker than those with h = 2n. Consequently, the scaling of the data, structure solution and refinement were challenging. The two molecules comprising the asymmetric unit are related by a noncrystallographic translation of ½ along a, but one of the molecules has two alternate positions related by a rotation of approximately 2°. This rotation axis is located near the edge of the central β‐sheet, causing a maximum distance disparity of 1.7 Å between equivalent atoms on the diametrically opposite side of the molecule. The crystal‐packing contacts are similar to two sequential combined unit cells along a of the previously determined monoclinic unit cell. Abnormally high final Rcryst and Rfree values (20.2% and 23.7%, respectively) are not unusual for structures containing pseudo‐translational symmetry and probably result from poor signal to noise in the weak h‐odd data.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S0907444910006797</identifier><identifier>PMID: 20445238</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Asymmetry ; ATOMS ; Carbonic anhydrase ; Carbonic Anhydrase II - chemistry ; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY ; crystal contacts ; CRYSTAL STRUCTURE ; Crystallization ; Crystallography, X-Ray ; CRYSTALS ; DIFFRACTION ; doubled axis ; Equivalence ; Human ; Humans ; MATHEMATICAL SOLUTIONS ; Models, Molecular ; MOLECULES ; ORIENTATION ; Protein Conformation ; Research Papers ; RESOLUTION ; ROTATION ; rotational disorder ; SCALING ; SHEETS ; SIGNALS ; STOWING ; SYMMETRY ; systematically weak data ; translational symmetry ; Translations ; Unit cell</subject><ispartof>Acta crystallographica. 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Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>The crystal structure of human carbonic anhydrase II with a doubled a axis from that of the usually observed monoclinic unit cell has been determined and refined to 1.4 Å resolution. The diffraction data with h = 2n + 1 were systematically weaker than those with h = 2n. Consequently, the scaling of the data, structure solution and refinement were challenging. The two molecules comprising the asymmetric unit are related by a noncrystallographic translation of ½ along a, but one of the molecules has two alternate positions related by a rotation of approximately 2°. This rotation axis is located near the edge of the central β‐sheet, causing a maximum distance disparity of 1.7 Å between equivalent atoms on the diametrically opposite side of the molecule. The crystal‐packing contacts are similar to two sequential combined unit cells along a of the previously determined monoclinic unit cell. Abnormally high final Rcryst and Rfree values (20.2% and 23.7%, respectively) are not unusual for structures containing pseudo‐translational symmetry and probably result from poor signal to noise in the weak h‐odd data.</description><subject>Asymmetry</subject><subject>ATOMS</subject><subject>Carbonic anhydrase</subject><subject>Carbonic Anhydrase II - chemistry</subject><subject>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</subject><subject>crystal contacts</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>CRYSTALS</subject><subject>DIFFRACTION</subject><subject>doubled axis</subject><subject>Equivalence</subject><subject>Human</subject><subject>Humans</subject><subject>MATHEMATICAL SOLUTIONS</subject><subject>Models, Molecular</subject><subject>MOLECULES</subject><subject>ORIENTATION</subject><subject>Protein Conformation</subject><subject>Research Papers</subject><subject>RESOLUTION</subject><subject>ROTATION</subject><subject>rotational disorder</subject><subject>SCALING</subject><subject>SHEETS</subject><subject>SIGNALS</subject><subject>STOWING</subject><subject>SYMMETRY</subject><subject>systematically weak data</subject><subject>translational symmetry</subject><subject>Translations</subject><subject>Unit cell</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkkFv1DAQhS0EomXhB3BBkTjAZcEeO3ZyQaoKlEVVOXTRtifLcRziktiLndDuv8dRylKERE8eab73PH4ehJ4T_IYQLN6e4xILxlhJMMZclOIBOiS0LJcYM_HwTn2AnsR4lSAAKh6jA8CM5UCLQ3RxPoRRD2MwmW8ylfXeed1ZZ3W29d2u92HbTp127JXLtAqVn3rKtbs6qGiy1Sq7tkObpLUfq87UqVI3Nj5FjxrVRfPs9lygrx8_rI8_LU-_nKyOj06XOucUloyJijSaCWANZcChAMNpAQpDYQSo9ASqDa1rwFo1ipTaaI55BVwICo2gC_Ru9t2OVW9qbdwQVCe3wfYq7KRXVv7dcbaV3_xPCQXPKS-SwcvZwMfByqjtYHSrvXNGDzLllRPAPFGvbq8J_sdo4iB7G7XpOuWMH6MUORWU5AzuJyklADkvE_n6vyQRosDAKJA_Q-7RKz8Gl4JNFGM8fSifsiAzpYOPMZhmHwPBctoY-c_GJM2Lu_ntFb9XJAHFDFzbzuzud5RHl-8v1_m0agu0nKU2DuZmL1Xhu0zTilxuzk4kbDZn_GKzlp_pL7nP2JM</recordid><startdate>201005</startdate><enddate>201005</enddate><creator>Robbins, Arthur H.</creator><creator>Domsic, John F.</creator><creator>Agbandje-McKenna, Mavis</creator><creator>McKenna, Robert</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7SP</scope><scope>7SR</scope><scope>7TK</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>H8D</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>201005</creationdate><title>Structure of a monoclinic polymorph of human carbonic anhydrase II with a doubled a axis</title><author>Robbins, Arthur H. ; Domsic, John F. ; Agbandje-McKenna, Mavis ; McKenna, Robert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5632-447b1fc4724f3426282e6382a028e72a1393ce3dd20cafa19cec606b267732f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Asymmetry</topic><topic>ATOMS</topic><topic>Carbonic anhydrase</topic><topic>Carbonic Anhydrase II - chemistry</topic><topic>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</topic><topic>crystal contacts</topic><topic>CRYSTAL STRUCTURE</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>CRYSTALS</topic><topic>DIFFRACTION</topic><topic>doubled axis</topic><topic>Equivalence</topic><topic>Human</topic><topic>Humans</topic><topic>MATHEMATICAL SOLUTIONS</topic><topic>Models, Molecular</topic><topic>MOLECULES</topic><topic>ORIENTATION</topic><topic>Protein Conformation</topic><topic>Research Papers</topic><topic>RESOLUTION</topic><topic>ROTATION</topic><topic>rotational disorder</topic><topic>SCALING</topic><topic>SHEETS</topic><topic>SIGNALS</topic><topic>STOWING</topic><topic>SYMMETRY</topic><topic>systematically weak data</topic><topic>translational symmetry</topic><topic>Translations</topic><topic>Unit cell</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Robbins, Arthur H.</creatorcontrib><creatorcontrib>Domsic, John F.</creatorcontrib><creatorcontrib>Agbandje-McKenna, Mavis</creatorcontrib><creatorcontrib>McKenna, Robert</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Aerospace Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Robbins, Arthur H.</au><au>Domsic, John F.</au><au>Agbandje-McKenna, Mavis</au><au>McKenna, Robert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of a monoclinic polymorph of human carbonic anhydrase II with a doubled a axis</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>2010-05</date><risdate>2010</risdate><volume>66</volume><issue>5</issue><spage>628</spage><epage>634</epage><pages>628-634</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>The crystal structure of human carbonic anhydrase II with a doubled a axis from that of the usually observed monoclinic unit cell has been determined and refined to 1.4 Å resolution. The diffraction data with h = 2n + 1 were systematically weaker than those with h = 2n. Consequently, the scaling of the data, structure solution and refinement were challenging. The two molecules comprising the asymmetric unit are related by a noncrystallographic translation of ½ along a, but one of the molecules has two alternate positions related by a rotation of approximately 2°. This rotation axis is located near the edge of the central β‐sheet, causing a maximum distance disparity of 1.7 Å between equivalent atoms on the diametrically opposite side of the molecule. The crystal‐packing contacts are similar to two sequential combined unit cells along a of the previously determined monoclinic unit cell. Abnormally high final Rcryst and Rfree values (20.2% and 23.7%, respectively) are not unusual for structures containing pseudo‐translational symmetry and probably result from poor signal to noise in the weak h‐odd data.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>20445238</pmid><doi>10.1107/S0907444910006797</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Acta crystallographica. Section D, Biological crystallography., 2010-05, Vol.66 (5), p.628-634 |
| issn | 1399-0047 0907-4449 1399-0047 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Asymmetry ATOMS Carbonic anhydrase Carbonic Anhydrase II - chemistry CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY crystal contacts CRYSTAL STRUCTURE Crystallization Crystallography, X-Ray CRYSTALS DIFFRACTION doubled axis Equivalence Human Humans MATHEMATICAL SOLUTIONS Models, Molecular MOLECULES ORIENTATION Protein Conformation Research Papers RESOLUTION ROTATION rotational disorder SCALING SHEETS SIGNALS STOWING SYMMETRY systematically weak data translational symmetry Translations Unit cell |
| title | Structure of a monoclinic polymorph of human carbonic anhydrase II with a doubled a axis |
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